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Q$$$b$N;YnCX-[b$PĵWP^;'8Nb$B]u{!\0E 'b$GT_ ~s'lb$lU.5+ b$Ԛ'~KۤDW$#b$}ۏha>ѧt4b$R-"҅N3b$zD _(x0Ҡ䈲 u b$y3]^>Ӵs3ϩ-Wb$U3v_ !@WWB$$b$|W\P_sE@b$Y8e+<9UH}I]b$%)Uvϥ$$Tb$7ؾ<Õ4d6b$G)+'k4+b$bEȨōƽ'g&b$ :<(Ϧc H;)H b$@`divN_d b$5d5,gf' 2$Plݬ** R$)mkRًt]G b$c\/$ZjR{. b$`4cliB5ܺ& 0AA f33@dg4mdmd<x: 0vppp@  <4!d!d@ 0t<4dddd@ 0tFg4dddd豒x: 00p p*R ʚ;85ʚ;<4dddd@U 0@r0___PPT10 2___PPT9/ 0?L, 8Covalent Inhibition KineticsO =O">-New Insights into Covalent Enzyme Inhibition  ., Synopsis  :The target enzyme: Epidermal Growth Factor Receptor (EGFR):; 5(EGFR kinase inhibitors in the test panel))%8Covalent inhibitors of cancer-related enzymes: Mechanism99*EGFR inhibition by covalent drugs: Example++'3Two steps: 1. non-covalent binding, 2. inactivation:4$Example experimental data: Neratinib%% .Algebraic method of data analysis: Assumptions>/ )6An alternate approach: Differential equation formalism:7 -BDynaFit paper  Citation analysis""*A "Kinetic Compiler" +)System of Simple, Simultaneous Equations `*,-DynaFit can analyze many types of experiments..&6The differential equation model of covalent inhibitionJ7 !'Model of covalent inhibition in DynaFit*(' "4Covalent inhibition in DynaFit: Data / model overlay*54 #0Covalent inhibition in DynaFit: Model parameters*10 ':Ki and kinact as distinct determinants of cellular potency;  ! $.(;Ki is a major determinant of cellular potency: Panel of 154H< 9 :4%Overall conclusions, up to this point*&% SxTHE NEXT FRONTIER: MICROSCOPIC  ON AND  OFF RATE CONSTANTSN='hConfidence intervals for  on /  off rate constants>5.2Likelihood profile method: Computational algorithm>3/"Likelihood profile method: Example>#zConfidence intervals for  on /  off rate constants: Results>>(1`Lower limits vs.  true values of rate constants010*hCellular potency vs. upper limit of  residence time H5 0X Residence time hypothesis of drug efficacy,-,+9Summary and conclusions: Biochemical vs. cellular potency,:!,AcknowledgmentsPSUPPLEMENTARY SLIDES,  7:CHECK UNDERLYING ASSUMPTIONS: BIMOLECULAR ASSOCIATION RATE,; xDifferential equation method: Example  Afatinib: Parameters==( <Varying assumed values of the association rate constant, kaIP=2 98Effect of assumed association rate constant: ConclusionsL9 'N1CHECK UNDERLYING ASSUMPTIONS: SUBSTRATE MECHANISM,2FSubstrate mechanism   Hit and Run L$ LSubstrate mechanism  Michaelis-Menten,'DSubstrate mechanism  Bi-Substrate,#  lSubstrate mechanism   Bi-Substrate : DynaFit notation,76 lSubstrate mechanism   Bi-Substrate : DynaFit notation,76/Presumed substrate mechanisms vs. kinact and Kit0",":Substrate mechanism  SummaryH5:THEORETICAL ASSUMPTIONS VIOLATED: CLASSIC ALGEBRAIC METHOD@;"ZCheck concentrations:  Tight binding or not?..;Check linearity of control progress curve ([Inhibitor] = 0)<<62ACRYLAMIDE WARHEAD: STRUCTURE VARIATION VS. kinact@3$ "2<Caveat: Small number of warhead structures in the test panel,=532Warhead structure type vs. inactivation reactivity33/C-D.E3J4K5L6M7O8P9QJcKdOfQgWjz{|}  0` ̙33` ` ff3333f` 333MMM` f` f` 3>?" dd@,|?" dd@   " @ ` n?" dd@   @@``PR    @ ` ` p>> ~(    6ݒ P  T Click to edit Master title style! !  0T   RClick to edit Master text styles Second level Third level Fourth level Fifth level!     S  0  ``  >*  0X `   R*(    0| `   F* H  0޽h ? ̙33 Default Design0 0 P@(  4 4 Npg| y y .  | x*a00aa 4 Nx| y y 3 . | z*a00aad 4 c $ ?  |4 4 N<{| y y 9 f | RClick to edit Master text styles Second level Third level Fourth level Fifth level!     S 4 T| y y r  | x*a00aa 4 Tx| y y r3  | z*a00aaH 4 0ηo~ ? ̙3380___PPT10.pU( xp\(  \ \ N< ]e]e      V* AAA \ NA ]e]e %     X* AAA \ TK ]e]e     V* AAA \ TU ]e]e %    X* AAAH \ 0ηo~ ? ̙3380___PPT10.CP) 0 0(  X  0A?`mXB  0D  $  <|W  >Petr Kuzmi , Ph.D. BioKin, Ltd.^      XB  0D000r  S <$|`0 |   <(| 0  d$December 5, 2014 Brandeis University$%   <x.|P&$ ^&Application to Anti-Cancer Drug Design''H  0޽h ? ̙33y___PPT10Y+D='  = @B +]  0 E = 0  :t  (  t x t c $|``  | XB t 0D`X t 0A?`mp 6t <|  : Cellular potency is driven mainly by the initial noncovalent binding. Chemical reactivity (covalent bond formation) plays only a minor role. Of the two components of initial binding: - the association rate constant has a dominant effect, but - the dissociation rate constant appears unimportant. These findings appear to contradict the widely accepted  residence time hypothesis of drug potency. *i-] 7t <|`}4 LFor a particular group of covalent (irreversible) protein kinase inhibitors:0M =z l P 8t  l P,$D  0 9t  0o"` P PSchwartz, P.; Kuzmic, P. et al. (2014) Proc. Natl. Acad. Sci. USA. 111, 173-178.Q  9 :t  <|l }@ ? REFERENCE H t 0޽h ? ̙33___PPT10+|D|' = @B D7' = @BA?%,( < +O%,( < +Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*8t %(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*8t D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*8t +  0  (  x  c $l|``  | XB  0D`"  C AF1file:///J:/fil/diary_dv10/2014/1412/141203/seminars/1411-brandeis/www/images/efgr-biology/F1.large.jpg"`p Y  <x|' _)http://ersj.org.uk/content/33/6/1485.full**Ll  wT,$D 0t2  6Ԕ"`;ZB  s *DԔ   <| . ~tyrosine kinase activityJl P     ,$D 0t  6Ԕ"`P   <$   :cancer  <4C ,$  0 f0kinase inhibitors act as anticancer therapeutics11H  0޽h ? ̙33  ___PPT10 +D_ ' = @B D ' = @BA?%,( < +O%,( < +D' =%(D' =%(D3' =4@BB BB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =-o6Bdissolve*<3<*D' =%(D' =%(D3' =4@BB BB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =-o6Bdissolve*<3<*D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*+8+0+0 +   0 vn(  x  c $P``   XB  0D`f  0A!?"`pFP l Lp Lp,$D 0t  6jJ"` pt2  6jJ"`@   <" L Jacrylamide  warhead functional group&& H  0޽h ? ̙335-___PPT10 +9D'  = @B D' = @BA?%,( < +O%,( < +D' =%(D' =%(D3' =4@BB BB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =-o6Bdissolve*<3<*+  0 .(  x  c $\x``   XB  0D`^  6VVf  0A ?"`P f2  0"``   <{ ^ ? protein chainz PQ     PPQ R ,$D 0n   0A"?"`PQ K    <n    Hirreversible inhibitorz @ P    P@  ,$D  0n   0A#?"`@ P   <p &  Acovalent adduct2  6jJ"`,$D 0H  0޽h ? ̙33  ___PPT10n +8|DR ' = @B D ' = @BA?%,( < +O%,( < +D' =%(D' =%(D3' =4@BB BB%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =-o6Bdissolve*<3<* Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<* D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<* D' =%(D' =%(D3' =4@BB BB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =-o6Bdissolve*<3<*+C  0L0 RJ (  x  c $`   XB  0D`X  0A?`mf  0A$?"` l  6."`0l   6."``    <  PMichael addition of a cysteine  SH group))    B {`  8Canertinib (CI-1033): experimental cancer drug candidate99 /H  0޽h ? ̙33y___PPT10Y+D='  = @B +  0  <(  x  c $``   XB  0D`^  6VVl  6A%1?"` z     ,$D 0t2  6jJ"`P"   <  Fbinding affinityl       ,$D 0t2   6jJ"`     <Х  Ichemical reactivity   <` u<,$  0 %Goal of the study: Evaluate the relative influence of binding affinity and chemical reactivity on cellular (biological) potency of each drug.x%H  0޽h ? ̙33  ___PPT10 +D_ ' = @B D ' = @BA?%,( < +O%,( < +D' =%(D' =%(D3' =4@BB BB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =-o6Bdissolve*<3<*D' =%(D' =%(D3' =4@BB BB%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =-o6Bdissolve*<3<* D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<* D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<* +8+0+ 0 +;  0 bZ (  x  c $``   XB  0D`^  6VVf  0A&?"``=  <DP] = [Inhibitor]    <  .NERATINIB VS. EFGR T790M / L858R DOUBLE MUTANT>/  3% 33$ XB  0D    <\ p0 <timeXB   0D @@   B0  Kfluorescence changeH  0޽h ? ̙33y___PPT10Y+D='  = @B +j  0 "    (  x  c $``   XB  0D`  04 @ D<4___PPT9  Control progress curve ([I] = 0) must be strictly linear - Negligibly small substrate depletion over the entire time course T*E  @`  <hD JCopeland R. A. (2013)  Evaluation of Enzyme Inhibitors in Drug Discovery , 2nd Ed., Eq. (9.1)(9.2)HcL    T ,   <@ tThe  textbook method (based on algebraic rate equations):0;     <@ @ ASSUMPTIONS:    6c ( 0 ,$ 0 +i2. Negligibly small inhibitor depletion - Inhibitor concentrations must be very much larger than Kinj9 g @`ll P  P ,$D  0ZB   s *DԔP P   <c 0 Y Both of these assumptions are violated in our case. The  textbook method of kinetic analysis cannot be used.$n4:H  0޽h ? ̙33___PPT10+hDt' c = @B D/' = @BA?%,( < +O%,( < +D' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =-o6Bdissolve*<3<* Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*+8+0+ 0 +  0  @(  x  c $c ``  c  XB  0D`X  0A?`m  <hc   \ NUMERICAL ENZYME KINETICS AND LIGAND BINDING*/. 33X  0A.?IP X  0A/?pB2f  0"`P`G   <#c  @  -Kuzmic, P. (2009) Meth. Enzymol. 467, 248-280^. ,5   <1c    -Kuzmic, P. (1996) Anal. Biochem. 237, 260-273^. H  0޽h ? ̙33y___PPT10Y+D='  = @B +h  0 (  x  c $9c ``  c  XB  0D`X  0A?`mX   0A3? \    <8Bc 0p[   892 citations 50-60 citations per year Most frequently cited in: Biochemistry (39%) J. Biol. Chem. (23%) J. Am. Chem. Soc. (9%) J. Mol. Biol. (5%) P.N.A.S. (4%) J. Org. Chem. (4%) ...      3             %  <xAc sp MAs of December 4, 2014:H  0޽h ? ̙33y___PPT10Y+D='  = @B +H  0  ''(  x  c $dXc ``  c  XB  0D`[z j   j ,$D 0;  0Zc J* T  G E + S ---> ES : k1 ES ---> E + S : k2 ES ---> E + P : k3 pH   3   `  0`   < dc pjf> JInput (plain text file):`B  0D C   <hc ,$D 0  d[E ] / dt = X n   08rc @,$D  0  - k1 [E] [S]X   0A?`m   <X|c   v0HOW DYNAFIT PROCESSES YOUR BIOCHEMICAL EQUATIONS*10 33R   s *A0` JX  00` z     ,$D 0,  <c    k1 [E] [S]`  0 z      ,$D 0  0Dc  z  k2 [ES]n 33333`  0  z l \   l  \ ,$D 0  0c  v J  k3 [ES]n `  0l \  z  `@@  ` @@,$D 0`B  0D j @  <(c  ` 4 = Rate terms: `B  0D @z @`@  `@@,$D 0`B  0D@@@  <dc &`4 ARate equations:`B  0D@R   <xc 0t ,$D   0 + k2 [ES] 33333N ! <c L < ,$D   0 + k3 [ES]| D " <c  p ,$D  0 d[ES ] / dt = X  $z ,   #  , ,$D   0B $ 0c <    + k1 [E] [S]& % <Tc ,\ 0  - k2 [ES] 33333" & <c 8   - k3 [ES]|  ' <hc  p ,$D   0 PSimilarly for other species...H  0޽h ? ̙33++___PPT10*+vD)' c = @B D=)' = @BA?%,( < +O%,( < +D4' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D4' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D4' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D4' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D4' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D4' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*%(DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* %(D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<* D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<* D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<* D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<* D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*!%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*!D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*!DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*"%(Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*#%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*#D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*#D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*'%(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*'D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*'+P+0+ 0 ++0+ 0 ++0+ 0 ++0+!0 ++0+"0 ++0+'0 +H  0 og//(  x  c $8c ``  c  XB  0D`[z j   j ,$ 0;  0D J* T  G E + S ---> ES : k1 ES ---> E + S : k2 ES ---> E + P : k3 pH   3   `  0`   < pjf> JInput (plain text file):`B  0D X   0A?`m   <    v0HOW DYNAFIT PROCESSES YOUR BIOCHEMICAL EQUATIONS*10 33R   s *A0` JX   00` z      ,$ 0,  <    k1 [E] [S]`  0 z      ,$ 0  0  z  k2 [ES]n 33333`  0  z l \   l  \ ,$ 0  0"  v J  k3 [ES]n `  0l \  z  `@@  ` @@,$ 0`B  0D j @  <*  ` 4 = Rate terms: `B  0D @z @`@  `@@,$ 0`B  0D@@@  <0 &`4 ARate equations:`B  0D@R  C *A1lego-001`  <4 p ."The LEGO method" of deriving rate equations</&X   0 R ! s *p R " s *p R # s *p t X $ 0 P R % s *P @ R & s *P 0 R ' s *P X ( 0l P \ R ) s * @ l R * s * 0 l R + s * l dB , <Dp0 0 dB - <Dp@ P @ dB . <Dp P  R / C *A2legologoZH  0޽h ? ̙33y___PPT10Y+D='  = @B +   0 4, (  x  c $XD ``    XB  0D`X  0A?`m5  <|F  OMASS ACTION LAW AND MASS CONSERVATION LAW IS APPLIED TO DERIVE DIFFERENT MODELS^P 3 3 3& 33  <`J X  o5Reaction progress Initial rates Equilibrium binding66  <(U ` BL  iFirst-order ordinary differential equations Nonlinear algebraic equations Nonlinear algebraic equationsjjLB  c $D  LB   c $D@    <d[  ` B EXPERIMENT    <`  ` SDYNAFIT DERIVES A SYSTEM OF ... H  0޽h ? ̙33y___PPT10Y+D='  = @B +  0 0 t(  tx t c $Hg ``    XB t 0D`l t 6A%1?"`P f t 0"` Ttz  2@ t 2 ,$D 0t t 6A(jJ?"`0 2@n t 0"`p `    t <n  4,$  0 NThis model is  integrated numerically .((H t 0޽h ? ̙33{ s ___PPT10S +@%~D ' m = @B D ' = @BA?%,( < +O%,( < +Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*t%(D' =+4 8?dCB0-#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*tD' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*tD{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* t%(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<* tD' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<* t+8+0+ t0 +3   0  L6(  Lx L c $t ``    XB L 0D`l L 6A%1?"`P f L 0A)?"`@ l L 6jJ"`-    L <w   d.DynaFit input  script :z f f  L  ff,$D 0t  L 6jJ"` P  ZB  LB s *DjJ    L <} f df dfixed constant:  rapid-equilibrium approximation &3#f L 0"` TH L 0޽h ? ̙335-___PPT10 +b'D'  = @B D' = @BA?%,( < +O%,( < +D' =%(D' =%(D3' =4@BB BB%(D' =1:Bvisible*o3>+B#style.visibility<* L%(D' =-o6Bdissolve*<3<* L+)  0 T(  Tx T c $ ``    XB T 0D`f T 0A*?"`@@A T < D ,$ 0 p,global fit: all curves are analyzed together(- !H T 0޽h ? ̙33___PPT10+'DO'  = @B D ' = @BA?%,( < +O%,( < +DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*T%(+8+0+T0 +!  0    \ (  \x \ c $ ``    XB \ 0D`l \ 6A+>?"`N. \ < p,D LDynaFit output window: \ <P   How do we get Ki out of this?H  \ <̣ :  ,$ 0 t Recall that kon was arbitrarily fixed at 100 M-1s-1 ( rapid equilibrium )L     <l2 \ 6jJ"`r2#z @  \ @,$D  0  \ B @  '1Ki = koff/kon = 0.341 / 100 = 0.00341 M = 3.4 nM2   $%t2  \ 6jJ"`` t2  \ 6jJ"` H \ 0޽h ? ̙33A9___PPT10+ZD'  = @B D' = @BA?%,( < +O%,( < +DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*\%(Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<* \%(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<* \D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<* \+8+0+\0 +  0 %  P| (  |x | c $l ``    XB | 0D`f | 0A,?"`  | <x ! 'Schwartz, Kuzmic, et al. (2014) Fig S10<(   7 | < d H ,$  0 CORRELATION ANALYSIS: Non-covalent initial binding affinity (R2 ~ 0.9) correlates more strongly with cellular potency, compared to chemical reactivity (R2 ~ 0.5).  # f | 0"` 0  | <$   dkinact(   | <0 <   hKi0 z D @   | D @ ,$D 0  | <`  E @  Lnon-covalent binding   | <d D  Gchemical reactivity Rz    |  ,$D 0~B | NDԔ0P0 ZB | s *D@` @ZB | s *D ~B | NDԔ  l | 6Ԕ"` ` pH | 0޽h ? ̙33, $ ___PPT10 +ɖ)D '  = @B Dk ' = @BA?%,( < +O%,( < +D' =%(D' =%(D3' =4@BB BB%(D' =1:Bvisible*o3>+B#style.visibility<* |%(D' =-o6Bdissolve*<3<* |D4' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<* |%(D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*|%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*|D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*|+8+0+|0 +   0 }p(  x  c $  ``    XB  0D`  <  0g 'Schwartz, Kuzmic, et al. (2014) Fig S11<(f  0A-?"`p P  <d F1j ,$  0 HNon-covalent Ki vs. Cellular IC50 strong correlation for a larger panelvI & :H  0޽h ? ̙33___PPT10+.rD'  = @B DD' = @BA?%,( < +O%,( < +D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*+8+0+0 +   0 2(  x  c $ ``   XB  0D`  < 0 (Non-covalent initial binding appears more important than chemical reactivity for the cellular potency of this particular panel of 11 covalent anticancer drugs.l8~l v v,$D  0`  0A?P 8  6# "` v 0Proc. Natl. Acad. Sci. USA. 111, 173-178 (2014).N1ZB  s *D8cH  0޽h ? ̙33___PPT10+ aD|' = @B D7' = @BA?%,( < +O%,( < +Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*+ j 0 p(  x  c $x0    XB  0D`X  0A?`mH  0޽h ? ̙33y___PPT10Y+D='  = @B +, d 0 Y Q   (  x  c $; ``   XB  0D`X  0A?`m  B= >"`0PB 6 We cannot determine  on and  off constants from currently available data. But we can estimate at least the lower limits of their confidence intervals.6p    0E J,$  0 nMETHOD:  Likelihood profile a.k.a.  Profile-t method8  l     ,$D  0  6N  D<4___PPT9 Watts, D.G. (1994) "Parameter estimates from nonlinear models Methods in Enzymology, vol. 240, pp. 23-36 Bates, D. M., and Watts, D. G. (1988) Nonlinear Regression Analysis and its Applications John Wiley, New York sec. 6.1 (pp. 200-216) - two biochemical examples ? (3H @`  6d_    = REFERENCES: H  0޽h ? ̙33{ s ___PPT10S +{֋D ' 3 = @B D ' = @BA?%,( < +O%,( < +D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<* D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<* +8+0+0 +  0  w(  x  c $W ``   XB  0D`X  0A?`m    <`q Mp D<4___PPT9 QPerform nonlinear least-squares fit with the full set of model parameters. Progressively increase a parameter of interest, P, away from its best-fit value. From now on keep P fixed in the fitting model. At each step optimize the remaining model parameters. Continue stepping with P until the sum of squares reaches a critical level. This critical increase marks the upper end of the confidence interval for P. Go back to step #2 and progressively decrease P, to find the lower end of the confidence interval. Z12 +V$(" @`   B   |Watts, D.G. (1994) "Parameter estimates from nonlinear models Methods in Enzymology, vol. 240, pp. 23-36 jk?      aH  0޽h ? ̙33y___PPT10Y+D='  = @B +  0 [ S   (  x  c $ ``   XB  0D`X  0A?`m  3 Z (confid-t001-002Confidence Interval    3 Z (confid-t001-002Confidence Interval    3 Z (confid-t001-002Confidence Interval   C `A (confid-t001-003Confidence Interval `   C `A (confid-t001-004Confidence Interval `   < d8 pAfatinib, replicate #1$  <ܡ     log (koff)B   <l     log (kinact)B dB  <D8c   B   Fsum of squares  << 0 T,$ 0 Dcritical level33l pN  pJ ,$D 0ZB  s *Dp@   <з  N  V lower end of confidence interval!! l  P Y  P Y,$D 0ZB  s *DP @ ZB  s *DP @   Bе  Y Qlower and upper end of C.I.H  0޽h ? ̙33P H ___PPT10( + D '  = @B D ' = @BA?%,( < +O%,( < +D' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =-o6Bdissolve*<3<*D' =%(D' =%(D3' =4@BB BB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =-o6Bdissolve*<3<*D' =%(D' =%(D3' =4@BB BB%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =-o6Bdissolve*<3<* +8+0+0 +  } 0   @ xc (  xx x c $ ``   XB x 0D`X x 0A?`md  x < "`,$D 0 kon: slope = -0.88n e  x <8 "`P p$ ,$D 0 koff: slope = ~0.05n  x <P `,$  0 h... association rate8   x < @  ,$  0 i... dissociation rate8 l x <@ p!0D,$  0 RCell IC50 correlates strongly with association rates. Dissociation has no impact.^Sb x C ,Acell-ic50"`@( l x 6V"`@  x <  V  3s H x 0޽h ? ̙33___PPT10+D'  = @B D:' = @BA?%,( < +O%,( < +D' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<* x%(D' =-o6Bdissolve*<3<* xD' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<* x%(D' =-o6Bdissolve*<3<* xD{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* x%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<* xD' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<* xD{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*x%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*xD' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*xD{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*x%(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*xD' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*x++0+ x0 ++0+ x0 ++0+ x0 ++0+x0 ++0+x0 +%  0 @X(  x  c $& ``  &  XB  0D`X  0A?`m   <&  ( We assumed that the lower limits for kon and koff are relevant proxies for  true values. One way to validate this is via Monte-Carlo simulations: 1. Simulate many articificial data sets where the  true value is known. 2. Fit each synthetic data set and determine confidence intervals. 3. Compare  true (i.e. simulated) values with lower limits.^   N   >'{ D  < &    ,$  0 l Preliminary Monte-Carlo results confirm our assumptions. Additional computations are currently ongoing.mmH  0޽h ? ̙33___PPT10+@D' $& = @B DD' = @BA?%,( < +O%,( < +D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*+8+0+0 +Y c 0 y q   (  x  c $,& ``  &  XB  0D`X  0A?`m  <& @,$ 0 0 Lower limit for  off rate constant defines the upper limit for residence time.tQP  <7& ~P;  Z Drug-receptor residence time : t = 1 / koffL.!)  <>& @,$ 0 H Both minimum koff and maximum t is invariant across our compound panel.lI  7  <pG& \ @0 ,$  0  This is unexpected in light of the  residence time theory of drug potency.DM$'   <N& ,E~ ,$ 0 9 However cellular IC50 varies by 3-4 orders of magnitude.2: $H  0޽h ? ̙33  ___PPT10` +>o{Dd ' V& = @B D ' = @BA?%,( < +O%,( < +DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*%(DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*%(DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* %(D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*++0+0 ++0+0 ++0+0 ++0+ 0 +   0   ^(  x  c $e& ``  &  XB  0D`X  0A?`m:   6f&   Copeland, Pompliano & Meek (2006) Nature Rev. Drug Disc. 5, 730 Tummino & Copeland (2008) Biochemistry 47, 5481 Copeland (2011) Future Med. Chem. 3, 1491#! , .T   <hv&  ASEMINAL PAPERS:   <{& <    JILLUMINATING DISCUSSION:   <&  p BEXAMPLE SYSTEMS:6  <& ,-  ^ work from Peter Tonge s lab (SUNY Stony Brook)00,=  <$& \ \0  3 Dahl & Akerud (2013) Drug Disc. Today 18, 697-707 `4 &H  0޽h ? ̙33y___PPT10Y+D='  = @B +.  D 0  a(   x  c $& ``  &  XB  0D`X  0A?`mN  0t& P D<4___PPT9 EQUILIBRIUM BINDING AFFINITY: Initial (non-covalent) binding seems more important for cell potency than chemical reactivity. BINDING DYNAMICS: Association rates seem more important for cell potency than dissociation rates (i.e.,  residence time ). x B ` @`  <H& @ s ,$  0 qCAVEAT: We only looked at 11 inhibitors of a single enzyme. Additional work is needed to confirm our findings.fr 3H  0޽h ? ̙33___PPT10+D' & = @B DD' = @BA?%,( < +O%,( < +D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<* D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<* +8+0+ 0 +u E 0 ]U (   x  c $& ``  &  XB  0D`X  0A?`m  <&   / Brion Murray Philip Schwartz* Jim Solowiej20 ,!X  0   <`&  } nPfizer Oncology La Jolla, CA6   <(& p 0  )* Currently Takeda Pharma San Diego, CA$*  ( l 0P   P 0,$D  0E   <& 0P $ =This presentation is available for download at www.biokin.comV>/f/   <& k vbiochemical kineticsF f    TB   c $D`@@H  0޽h ? ̙33___PPT10+k=GD|' = @B D7' = @BA?%,( < +O%,( < +Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<* D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<* + g 0 @p(  x  c $x& `  &  XB  0D`X  0A?`mH  0޽h ? ̙33y___PPT10Y+D='  = @B +  0 p(  x  c $& `  &  XB  0D`X  0A?`mH  0޽h ? ̙33y___PPT10Y+D='  = @B + z 0 0 (  `(  ` `  Hx&  ?"```  &  ^B ` 6D?`l ` 6A??"``m ` BD' ?"` bDYNAFIT-GENERATED OUTPUT. Z ` B' ?"`\ 6  Ki = kdI / kaIr6r ` <A >??"`@    ` B' ?"`| XV  -kaI = 10 M-1s-1 ... assumed (fixed constant).+ ` BL' GHj "``@ yrecall: we assumed this value@ ~ ` < '   ,$  0 xCould the final result be skewed by making an arbitrary assumption about the magnitude of the association rate constant?Jy.  6H ` 0޽h ?` ̙33___PPT10+MdD' #' = @B DD' = @BA?%,( < +O%,( < +D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*`%(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*`D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*`+8+0+`0 +`) P 0 `](  x  c $.' ``  '  XB  0D`X  0A?`mr  <A >??"` ?  <0' >  kaI, M-1s-1d    LB  c $D`P LB  c $D pp    <8' `Zd =ASSUMED   <p='  *T  > 10 20 40    <P?'   !EXAMPLE: Afatinib, Replicate #1/3$"  l ` `,$D  0   <HD' P `W4 JDETERMINED FROM DATA   <H'  W  kdI, s-1J    <TO'     kinact, s-1J  TB  c $Dp  <V'   Ki, nMJ F  <]'  kinact/Ki, M-1s-1      <f'  N ,$ 0 H0.0016 0.0016 0.0016  <,l'   ,$ 0 I0.037 0.074 0.148  <p'  [  ,$ 0 ? 3.7 3.7 3.7  <t'  V ' ,$  0 Ki = kdI / kaI6  <'   ,$ 0 B23.1 23.1 23.1H  0޽h ? ̙33;3___PPT10+*uD' ' = @B D' = @BA?%,( < +O%,( < +Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*D' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =-o6Bdissolve*<3<*D' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =-o6Bdissolve*<3<*D' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =-o6Bdissolve*<3<*D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*D' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =-o6Bdissolve*<3<*++0+0 ++0+0 ++0+0 ++0+0 ++0+0 + Q 0     (  x  c $(' ``  '  XB  0D`X  0A?`m  <' "` nThe assumed value of the  on rate constant does effect the best-fit value of the dissociation ( off ) rate constant, kdI. The fitted value of kdI increases proportionally with the assumed value of kaI. Therefore the best-fit value of the inhibition constant, Ki, remains invariant. The inactivation rate constant, kinact, remains unaffected.*.2-"     = % by4=7l      ,$D  0ZB  s *D|    <|' d   >Assumptions about the  on rate constant have no effect on the best-fit values of kinact, Ki, and kinact/Ki.n. >S    <' < ,$  0 However, the dissociation ( off ) rate constant remains undefined by this type of data.DX H  0޽h ? ̙33{ s ___PPT10S +;D ' ' = @B D ' = @BA?%,( < +O%,( < +Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*%(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<* D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<* +8+0+ 0 + f 0  p(  x  c $' `  '  XB  0D`X  0A?`mH  0޽h ? ̙33y___PPT10Y+D='  = @B +V J 0 }u  (   x  c $' ``  '  XB  0D`X  0A?`m-  <'  EASSUMING THAT THE MICHAELIS COMPLEX CONCENTRATION IS EFFECTIVELY ZERO`F 3 3 3 33h  c 2AegfrHR"`` 5  <' 3f"`T `0  v Justified by assuming that [S]0 << KM In our experiments KM e" 220 M and [S]0 = 13 M The model was used in Schwartz et al. 2014 (PNAS) @ H  0޽h ? ̙33y___PPT10Y+D='  = @B + K 0  t(   x  c $0' ``  '  XB  0D`X  0A?`m  <,*  <ASSUMING THAT ATP COMPETITION CAN BE EXPRESSED THROUGH  APPARENT KivE 3 3 3  3 33Bh  c 2AegfrMM"`m   <H * 3f"` E  b  S is the peptide substrate All inhibitors are ATP-competitive Therefore they are  S -noncompetitiverk  H  0޽h ? ̙33y___PPT10Y+D='  = @B + L 0  (   x  c $<* ``  *  XB  0D`X  0A?`mh  c 2AegfrBS"``p  <* 3f"` `  4 Catalytic mechanism is  Bi Bi ordered ATP binds first, then peptide substrate  I is competitive with respect to ATP  I is (purely) noncompetitive w.r.t.  S Substrates are under  rapid equilibrium T 1H  0޽h ? ̙33y___PPT10Y+D='  = @B += { 0 h (  hx h c $.* ``  *  XB h 0D`X h 0A?`mn h 6/* "`D,$  0 :[mechanism] E + ATP <==> E.ATP : kaT kdT*; .> h <P7* p D DDYNAFIT INPUT:f  h 0A?"` |  h 0A?"`" ,$D 0_  h B4?* +,$  0 - S + E.ATP <==> S.E.ATP : kaS kdS..P LB  h c $Dp   h 0A?"`P e,$D 0 h <F* Z0h @ MECHANISM: * h BJ* m-,$  0 $S.E.ATP ---> P + E + ADP : kcat%%$ h 0A?"`W ,$D 0 h BHP*  R ,$  0 t*E + I <==> E.I : kaI kdI+++ h 0A?"`  ,$D  0, h BU*  Fp ,$   0 &E.I ---> E-I : kinact''$ h <Y* D P,$   0 e3Similarly for the remaining steps in the mechanism.44H h 0޽h ? ̙33/|/___PPT10\/+_* D-' h* = @B D-' = @BA?%,( < +O%,( < +D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*h%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*hD' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*hDn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<* h%(D' =+4 8?dCB0-#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<* hD' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<* hD{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* h%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<* hD' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<* hDn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<* h%(D' =+4 8?dCB0-#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<* hD' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<* hD{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*h%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*hD' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*hDn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*h%(D' =+4 8?dCB0-#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*hD' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*hD{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*h%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*hD' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*hDn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*h%(D' =+4 8?dCB0-#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*hD' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*hD{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*h%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*hD' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*hD{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*h%(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*hD' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*h+P+0+h0 ++0+ h0 ++0+h0 ++0+h0 ++0+h0 ++0+h0 +  | 0 kc  p(  px p c $y* ``  *  XB p 0D`X p 0A?`m p <x* @P} KDYNAFIT INPUT WINDOW:f p 0A?"``@l p 6jJ"` l [``  p`[` ,$D 0n p 0A?"`p`` t p 6"`[ {t p 6"`  H p 0޽h ? ̙335-___PPT10 +D'  = @B D' = @BA?%,( < +O%,( < +D' =%(D' =%(D3' =4@BB BB%(D' =1:Bvisible*o3>+B#style.visibility<*p%(D' =-o6Bdissolve*<3<*p+% M 0  (   x  c $d* ``  *  XB  0D`X  0A?`m   <*   !EXAMPLE: AFATINIB, REPLICATE #1/3@"  3 33 f  0A?"` 4  <@z*    kaI, M-1s-1d      <~* $ 9FIXEDLB  c $D@0@  < w*   kdI, s-1J    <*  m  kinact, s-1J    <* vA  ^*Hit-and-Run Michaelis-Menten Bisubstrate++LB  c $D0`   <`* K ,$ 0 U 10 10 160* 5  <,*  Q ,$  0 [ATP]/KM,ATP = 16F LB  c $D` 0`   <ط* v ,$ 0 G0.031 0.033 0.032  <*  K ,$ 0 J0.0019 0.0019 0.0019l h`   h` ,$D  0TB   c $D0`    <*  Ki, nMJ    B*  kdI/kaIF  )   <* h  3.1 3.1 0.19 = 3.1/16   H  0޽h ? ̙33 ___PPT10+߰*D' * = @B D' = @BA?%,( < +O%,( < +D' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =-o6Bdissolve*<3<* D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<* D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<* D' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =-o6Bdissolve*<3<* D' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =-o6Bdissolve*<3<* Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<* D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<* ++0+ 0 ++0+ 0 ++0+ 0 ++0+ 0 +  O 0   @ P (   x  c $ * ``  *  XB  0D`X  0A?`m  <* P D<4___PPT9 Basic characteristic of inhibitors (Ki, kinact) are essentially independent on the presumed substrate mechanism. The inactivation rate constant (kinact) is entirely invariant across all three substrate mechanisms. The initial binding affinity (Ki) needs to be corrected for ATP competition in the case of  Hit and Run and  Michaelis-Menten mechanisms: - Hit-and-Run or Michaelis-Menten: Divide the measured Kiapp value by [ATP]/KM,ATP to obtain true Ki - Bisubstrate: True Ki is obtained directly.V$   G F P    $d^ @`H  0޽h ? ̙33y___PPT10Y+D='  = @B +  0 p(  x  c $)= `  =  XB  0D`X  0A?`mH  0޽h ? ̙33y___PPT10Y+D='  = @B +  0 0 4(  4x 4 c $0= ``  =  XB 4 0D`f 4 0A&?"`0   4 <1=   A [Inhibitor] l 4 68c"`z pr  4 pr ,$D  0 4 <"= r  W[Enzyme] 20 nM, ZB  4 s *DjJ``ZB  4 s *DjJ```B  4B 0DjJp```$  4 0* T \,$ 0 BThe assumption that [Inhibitor] >> [Enzyme] clearly does not hold.2C  4 <"=  & ,$ 0 We have  tight binding , making it impossible to utilize the classic algebraic method.LW >H 4 0޽h ? ̙33  ___PPT10 +nn*D ' G= = @B D ' = @BA?%,( < +O%,( < +Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*4%(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*4D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*4DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* 4%(DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* 4%(+p+0+ 40 ++0+ 40 +!  0 H@ $(  $x $ c $N= ``  =  XB $ 0D`f $ 0A'?"` |  $ <O= 0  This  slight nonlinearity has a massive impact, making it impossible to utilize the classic algebraic method:pp  $ <U= 6 < REFERENCE:   $ <Y=  @  >`Kuzmic et al. (2015)  An algebraic model for the kinetics of covalent enzyme inhibition at low substrate concentrations Anal. Biochem., in press Manuscript No. ABIO-14-632   m       )l  $ 6jJ"`  P H $ 0޽h ? ̙33y___PPT10Y+D='  = @B +  0 p(  x  c $@  H  0ηo~ ? ̙33. 0 @ x >(  x ^ x S 4   =  x c $L49 f  =  4 H x 0ηo~ ? ̙3380___PPT10.P 0  ((   ^  S 4     c $ 49 f    H  0ηo~ ? ̙3380___PPT10.P 0  ((   ^  S 4     c $Џ 49 f    H  0ηo~ ? ̙3380___PPT10.P 0  ((   ^  S 4     c $ 49 f    H  0ηo~ ? ̙3380___PPT10.P 0  ((   ^  S 4     c $| 49 f    H  0ηo~ ? ̙3380___PPT10.P 0  ((   ^  S 4     c $ 49 f    H  0ηo~ ? ̙3380___PPT10.P 0  ((   ^  S 4   |  c $|49 f  |  H  0ηo~ ? ̙3380___PPT10.P 0 P ((   ^  S 4     c $d 49 f    H  0ηo~ ? ̙3380___PPT10.P 0 p((  ^  S 4     c $, 49 f    H  0ηo~ ? ̙3380___PPT10.P 0  ((   ^   S 4      c $ 49 f    H   0ηo~ ? ̙3380___PPT10.P 0 ((  ^  S 4     c $ 49 f    H  0ηo~ ? ̙3380___PPT10.P 0 ((  ^  S 4     c $0 49 f    H  0ηo~ ? ̙3380___PPT10.P 0 0((  ^  S 4     c $` 49 f    H  0ηo~ ? ̙3380___PPT10.P 0 P((  ^  S 4     c $0 49 f    H  0ηo~ ? ̙3380___PPT10.P 0 ((  ^  S 4     c $ 49 f    H  0ηo~ ? ̙3380___PPT10.P  0 d((  d^ d S 4    d c $ 49 f    H d 0ηo~ ? ̙3380___PPT10.P  0 l((  l^ l S 4    l c $ 49 f    H l 0ηo~ ? ̙3380___PPT10.P  0 0t((  t^ t S 4    t c $ 49 f    H t 0ηo~ ? ̙3380___PPT10.P 0 P|((  |^ | S 4    | c $? 49 f    H | 0ηo~ ? ̙3380___PPT10.P. 0 >(  ^  S 4     c $x 49 f   4 H  0ηo~ ? ̙3380___PPT10.P. 0 >(  ^  S 4   =   c $= 49 f  =  4 H  0ηo~ ? ̙3380___PPT10.P 0 ((  ^  S 4   =   c $= 49 f  =   H  0ηo~ ? ̙3380___PPT10.Y aF6, 0 |(  d  c $4     3 rd ss49 f    H  0ηo~ ? ̙33 0 ((  ^  S 4     c $ 49 f    H  0ηo~ ? ̙3380___PPT10.Y aF6 0 ((  ^  S 4     c $ 49 f    H  0ηo~ ? ̙3380___PPT10.Y aF6 0  ((   ^   S 4      c $t 49 f    H   0ηo~ ? ̙3380___PPT10.Y aF6 0 (((  (^ ( S 4    ( c $d 49 f    H ( 0ηo~ ? ̙3380___PPT10.Y aF6 0 @8((  8^ 8 S 4    8 c $Ԕ 49 f    H 8 0ηo~ ? ̙3380___PPT10.Y aF6! 0 P((  P^ P S 4    P c $< 49 f    H P 0ηo~ ? ̙3380___PPT10.Y aF6" 0 X((  X^ X S 4    X c $ 49 f    H X 0ηo~ ? ̙3380___PPT10.Y aF6# 0 `((  `^ ` S 4    ` c $ 49 f    H ` 0ηo~ ? ̙3380___PPT10.Y aF6& 0 @x((  x^ x S 4    x c $0M 49 f    H x 0ηo~ ? ̙3380___PPT10.Y aF6' 0 `((  ^  S 4     c $d% 49 f    H  0ηo~ ? 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