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(                      &1:D>phs?"-(./H&D$        5    ,*&:#$c+    D# (#'609 <o02  9"7G55H#;  &  (# F (0 '9  8  # # (   G0   *+D :(/  s  + 1'>*/53*    =6          "        Lb$C8B~.~k]%$b$8 Ze|b$>|W\P_sE@ ~b$TMJ-3 b$RS{%L<b$8wN0B:MU?*?-b$sMMxő]UX/mb$7N҉ X S\b$Y8e+<9UH}I]|b$9"HCOe(Ub$%)Uvϥ$$vZb$7ؾ<Õ4~b$G)+'k4+b$bEȨōƽ'gH)b$>3=t̏3Kb$ :<(Ϧc H;~ 0AA f33@dg4OdOdx: 0ppp@  <4!d!d@ 0t<4BdBd@ 0tg4ddddx: 0p p25T ʚ;t8ʚ;<4dddd@U 0@r0___PPT10 2___PPT9/ 0?\, HBinding Constants & Mechanisms pt. 3O =>  -Covalent inhibitors of cancer-related enzymes.. !EGFR inhibition by covalent drugs"" 3Two steps: 1. non-covalent binding, 2. inactivation:4$Example experimental data: Neratinib%% \ Textbook method of data analysis: The Recipe//^ Textbook method of data analysis: Assumptions,0"%Check linearity: Entire control curve&&+Check linearity: The first ten minutes only,,ZCheck concentrations:  Tight binding or not?..,Summary of checks on theoretical assumptions--!Three possible ways to proceed#.Traditional method of analysis: Determine kobs8/* *'4Traditional method of analysis: Determine kinact, Kid5*  ,*--Determine kinact, Ki from separate replicates.    , %3Is the problem in the poor quality of the raw data?*43 )*Is the problem with the assumed mechanism?*+* +.The kobs plot suggests a single-step mechanismh/    './Initial rate data suggests a two-step mechanismJ0  16Binding affinity of initial complex from initial rates*76 3/Traditional method of kinetic analysis: Summary*0/ 7+Traditional method of analysis: Post mortem8,   5!Two more possible ways to proceed""86The differential equation model of covalent inhibition*76 ;'Model of covalent inhibition in DynaFit*(' =4Covalent inhibition in DynaFit: Data / model overlay*54 >0Covalent inhibition in DynaFit: Model parameters*10 M0Compare with binding affinity from initial rates*10 N?Reproducibility of Ki & kinact determinations: Numerical method@  ! ,"Q3Compare results with the classical algebraic method*43 SBut what can you do with this?* X:Ki and kinact as distinct determinants of cellular potency;  ! $.Z?Ki and kinact as determinants of cellular potency: Panel of 154f@  2 $3VSummary and conclusions* UAcknowledgments/C     "$&(*,/02 4!6"9#:$<%?&@'O.P/R0T1W2Y3[4  0` ̙33` ` ff3333f` 333MMM` f` f` 3>?" dd@,|?" dd@   " @ ` n?" dd@   @@``PR    @ ` ` p>> ~(    6` P  T Click to edit Master title style! !  0L   RClick to edit Master text styles Second level Third level Fourth level Fifth level!     S  0 ``  >*  0P `   R*(    0 `   F* H  0޽h ? ̙33 Default Design0 0 P@(  4 4 N2 y y .    x*a00aa 4 NC y y 3 .   z*a00aad 4 c $ ?   4 4 NdF y y 9 f   RClick to edit Master text styles Second level Third level Fourth level Fifth level!     S 4 TS y y r    x*a00aa 4 T T y y r3    z*a00aaH 4 0ηo~ ? ̙3380___PPT10.pU( xp\(  \ \ NPIU ]e]e    U  V* AAA \ NNU ]e]e %   U  X* AAA \ TLXU ]e]e   U  V* AAA \ TdaU ]e]e %  U  X* AAAH \ 0ηo~ ? ̙3380___PPT10.CP) 0 ( 0(     6   = Determination of Binding Affinities and Molecular MechanismsL>$3333XB  0D  <@    0Petr Kuzmi  BioKin, Ltd.>    XB  0D0,  <    ^Part 3: Case study  Covalent Enzyme InhibitorsF0   C \A0BS_bannerThe Biochemical Society c   < 0  a!Training Day May 2, 2014 (London)$" H  0޽h ? ̙33y___PPT10Y+D=' p = @B +  0 P  M(   x  c $ ``   XB  0D`^  6VV3  <  MCOVALENT INHIBITION WORKS BY MAKING A PERMANENT CHEMICAL BOND WITH THE ENZYME^N& 3  3 3 33f  0A?"`P f2  0"``   <  ^ ? protein chainl PQ    PPQ R ,$D 0n   0A?"`PQ K    <     Hirreversible inhibitorl @ P   P@  ,$D  0n   0A?"`@ P    <l  &  Acovalent adduct2  6jJ"`,$D 0H  0޽h ? ̙33  ___PPT10n +$ADR ' = @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<* +?  0L0 NF  (   x  c $ `   XB  0D`X  0A?`mJ  0 "` Schwartz, P.; Kuzmic, P. et al. (2014)  Covalent EGFR inhibitor analysis reveals importance of reversible interactions to potency and mechanisms of drug resistance Proc. Natl. Acad. Sci. USA. 111, 173-178. Issue 1, January 7 *  <,2)f  0A?"``   <|ƒ  :EXAMPLE: H  0޽h ? ̙33y___PPT10Y+D=' p = @B +  0 SKp   (   x  c $Β ``   XB  0D`^  6VVl  6A1?"` l k   k ,$D 0t2   6jJ"`P"    <В k  ^equilibrium binding constant&   <  f|$  0H@___PPT9" /Kinetic assay: Mix enzyme (E) + substrate (S) + inhibitor (I) Continuously observe the appearance of product (P) over time Analyze the [Product] vs. time data to determine Ki and kinact   2=  , @`H  0޽h ? ̙33___PPT10+nKDt'  = @B D/' = @BA?%,( < +O%,( < +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 SK   (   x  c $O ``   XB  0D`^  6VVf   0A?"``=   <`Q DP] = [Inhibitor]     <E   .NERATINIB VS. EFGR T790M / L858R DOUBLE MUTANT>/  3% 33$ XB   0D   <[ \ p0 <timeXB  0D @@  B: 0  Kfluorescence change  <@X    }%Schwartz, Kuzmic et al. (2014) Fig S8<&H  0޽h ? ̙33y___PPT10Y+D=' p = @B +  0  $ 6(  $ x $ c $ l ``   XB $ 0D` $ <tc P", v1. Fit fluorescence vs. time to an exponential equation  kobs values K#   ; ( $ <s M PTHIS METHOD ASSUMES THAT THE INHIBITION INDEED PROCEEDS IN TWO CONSECUTIVE STEPSPQ; 3 3 33 $ < :  MTHE TRADITIONAL RECIPE: $ < (` JCopeland R. A. (2013)  Evaluation of Enzyme Inhibitors in Drug Discovery , 2nd Ed., Eq. (9.1)(9.2)HcL    T kl  ]  $ # ,$D 0x $  S A  ??#" `?   o $  <  0 ]  Mt ... time vi ... initial reaction rate kobs ... first-order rate constantpN        * v $  c &A  ??#" `?@  $ B   zF ... fluorescence signal at time t F0 ... instrument baseline rP ... concentration-to-signal scaling parameter [P] ... product concentration at time t"      W   @Y^ $ 6:l  , ) $ , ),$D  0> $  <X  ,   2. Fit  kobs vs. [Inhibitor] to a hyperbolic equation kinact and Ki I   >-x $  S A  ??#" `? ) H $ 0޽h ? ̙33___PPT10+ D' = @B Ds' = @BA?%,( < +O%,( < +D4' =%(D' =%(D' =4@BBBB%(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<*$ +   0 0 4 ?(  4 x 4 c $4 ``   XB 4 0D`^  4 6 4 0 $ D<4___PPT9 IKControl progress curve ([I] = 0) is strictly linear - Negligibly small substrate depletion over entire time course - Absence of product inhibition, enzyme deactivation, etc. Negligibly small inhibitor depletion - Inhibitor concentrations are very much larger than [Enzyme] - Inhibitor concentrations are very much larger than KiL$|sI @`N 4 B  0 ,$  0 In other words: - The inhibitor is not  tight binding . - The mole fraction of unbound inhibitor does not change over time.~* n 4 <  THE  TRADITIONAL RECIPE RELIES ON SEVERAL IMPORTANT THEORETICAL ASSUMPTIONSNM5 3  3  33H 4 0޽h ? ̙33___PPT10+cD'  = @B DD' = @BA?%,( < +O%,( < +D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*4 %(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*4 D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*4 +8+0+4 0 +<  0  , (  , x , c $ ``   XB , 0D` , <  ! ?DynaFit script: ./published/Schw1473/Nera/01-fit-control-R1.txt4@  0 f , 0A ?"`  , <X @,$  0 T"Is this  linear ? , <, p@uD,$  0 n<Is this  sufficiently linear? , < 9  @,$ 0 IOpinions will vary...H , 0޽h ? ̙33  ___PPT10 + eD '  9 = @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<*, 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@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<*, %(D' =-o6Bdissolve*<3<*, ++0+, 0 ++0+, 0 ++0+, 0 +x  0 P < {(  < x < c $9 ``  9  XB < 0D` < <P9  ! ?DynaFit script: ./published/Schw1473/Nera/02-fit-control-R1.txt4@  0  < <9 pP IMost definitely linear.f  < 0A ?"` =D  < 69 p0r,$  0 xBut it s only 50% of the data trace... Still OK to proceed?== < <L9 ` p4 ,$ 0 IOpinions will vary...H < 0޽h ? ̙335 - ___PPT10 +{D' %9 = @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<* < D' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<*< %(D' =-o6Bdissolve*<3<*< +p+0+ < 0 ++0+< 0 +v  0 \Tp  D (  D x D c $/9 ``   XB D 0D`f D 0A?"`0    D <19   A [Inhibitor] l  D 68c"`l pr  D pr ,$D  0  D  <(79 r  y[Enzyme] 20 nM,  ZB  D s *DjJ``ZB  D  s *DjJ```B D B 0DjJp```$ D 0=9 T \,$ 0 BThe assumption that [Inhibitor] >> [Enzyme] clearly does not hold.2Ct D <C9  >,$ 0 xWe have  tight binding , which is not supposed to happen...@=$ H D 0޽h ? ̙33  ___PPT10 +6^ND ' L9 = @B D ' = @BA?%,( < +O%,( < +Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*D %(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*D D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*D DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*D %(DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*D %(+p+0+D 0 ++0+D 0 +G   0  L z(  L x L c $`U9 ``  9  XB L 0D`k L <+B#style.visibility<*L %(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*L D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*L +8+0+L 0 +  0    T ~(  T x T c $t{9 ``  9  XB T 0D` T <@9  U1. Change the assay: throw out this data and go back to the lab -linearity: can we find conditions where [S] >> KM? -tight binding: can we find conditions where [E] << [I]?v/ '  + @` T <9 P3 ,$  0 2. Change the method of data analysis: -use a differential equation model instead of simple algebra -that method makes no simplifying assumptions of any kindB% [ @` T <p9 p ,$  0 %3. Cross your fingers and hope for a meaningful result -use the traditional algebraic method anyway -this is the path of least resistance (no changes required)R8 ; @`4  T B9 GN H0 "`@,$D 0 $maybe... but how long would it take?@%      T <9 "` ,$D 0 ,H T 0޽h ? T  ̙33qi___PPT10I+N$DM' 9 = @B D' = @BA?%,( < +O%,( < +D' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<* T %(D' =-o6Bdissolve*<3<* T D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*T %(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*T D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*T D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*T %(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*T D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*T DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* T %(++0+T 0 ++0+T 0 ++0+ T 0 ++0+ T 0 +  0    \  (  \ x \ c $9 ``  9  XB \ 0D` \ <9    LDynaFit script: ./published/Schw1473/Nera/04-determine-kobs-R1, -R2, -R3.txt4M  =   \ <x9  DDynaFit input: l  30 \  30,$D  0n \  0A?"` Z30  \  <9   ADynaFit output:  \  <9     b[I] = 31.25 nM   \  <L9  s  >kobs = (6.6 0.7) 10-3 s-1   \ <9  0  [task] data = generic task = fit [parameters] t, vi, kobs, Fo, rP [model] kobs = 0.001 ? vi = 0.001 ? Fo = 0 ? rP = 5000 P = (vi/kobs) * (1 - exp(-kobs*t)) F = Fo + rP*P nU):?   \ <9 p D,$  0 _-Repeat this for all inhibitor concentrations...H \ 0޽h ? ̙33{ s ___PPT10S +D ' 9 = @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@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 e ] 0 t  (  t x t c $9 ``  9  XB t 0D` t <=   ADynaFit script: ./published/Schw1473/Nera/05-fit-kobs-average.txt4B  2  t <=  DDynaFit input:l 1 t 1,$D  0n t  0A?"`1 t  < =  qX ADynaFit output: t  <=  p0 kinact = (0.010 0.019) s-1>    t  <P=  `  Ki = (420 850) nM>  $Pl b$ t b$,$D 0z2 t  <8c"` RBz2 t  <8c"`b$R t  B|= @  VThese results are meaningless. t <"=     [task] data = generic task = fit [parameters] I, kinact, Ki [model] kinact = 1 ? Ki = 1 ? kobs = kinact * I / (I + Ki) JO ;    H t 0޽h ? ̙33___PPT10+:7[D' = @B Ds' = @BA?%,( < +O%,( < +Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*t %(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*t D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*t D4' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*t %(+  0     (   x  c $<5= ``  =  XB  0D`  <6=   FDynaFit script: ./published/Schw1473/Nera/05-fit-kobs-R1, -R2, -R3.txt4G  7 V  <D== ` &There were three separate experiments (three 96-well plates). Let s try to average the three best-fit values of kinact and Ki, one from each plate:tp  ,p l `WD   `WD ,$D 0TB   c $DD TB   c $D    <J= `H  Z(replicate #1 replicate #2 replicate #3))4   <P=  d "1000 kinact, s-1`    TB   c $D0 0 D    <W=   d Ki, nM6 $h   <@^= HW  & 1.6 53 6.1 253 27.7 > 1000000'   <@j=  ,$  0 nThis is not helping...< H  0޽h ? ̙33A9___PPT10+_D' q= = @B D' = @BA?%,( < +O%,( < +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?\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 j b  d (  d x d c $x= ``  =  XB d 0D`X  d 0A? d <z=  THIS NERATINIB CONCENTRATION PRODUCED THE  WORST REPLICATE OF KOBS@D@ 3 33, 1 d B= ~8> Bkobs = (0.66 0.07) 10-3 s-1 " LB d c $D3f  d B= : Bkobs = (1.18 0.07) 10-3 s-1 " LB d c $D^ ^  d <= 4~,$  0 Data are  as good as they will ever get with this particular assay. However, the kobs estimates vary up to 100%. This isn t good.>R -R-H d 0޽h ? ̙33___PPT10+MdD' = = @B DD' = @BA?%,( < +O%,( < +D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*d %(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*d D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*d +8+0+d 0 +p!  0 P 0<| (  | x | c $x= ``  =  XB | 0D` | <= \s d 0Mechanism  A : two steps<   | <,= 8z  7E + IRB | s *D6 | <H= h \Ki$   | <Ļ= 8\  OEIRB "| @ s *D $| < = Vd OEI^B %| 6DjJJ &| <,= @ d OE~I '| <= P `kinact$ RB (| s *D` ` RB )| s *D` @f2 +| 0"`  ,| <4= Pf$ ;[I] -| <D=  X  jkobs0f2 .| 0"` / #f2 /| 0"`T f2 0| 0"`3f2 1| 0"`/' 2| <=   maximum kobs = kinactV  ,RB 3| s *D` @g l `p 9| 0 `,$D 0  |  B8=  A  4Mechanism  B : single step< `B  | 0D  `B  |  0D  |  B= @| P  7E + IlB |  <DjJ *  |  B|= E j  ]k1 >   |  B= | D P  OE~I`B | 0D H t2 |  6"` <  |  BD%  &p ;[I] |  B% Z   jkobs0t2 |  6"`K X t2 |  6"` ) t2 |  6"` G t2 |  6"`:i y E |  B = H P  no maximum slope = kinact/Kip fB 4|  6D|`RB 5| s *D` RB 6| s *D   7| <<%  [x half-maximum [I] = Ki<f2 :| 0"`@f2 ;| 0"`0o^ <| <%   *KOBS PLOTS ARE EITHER HYPERBOLIC OR LINEAR+ 3 3 3  3 3 3 33'H | 0޽h ? ̙33~___PPT10^+IDB' p = @B D' = @BA?%,( < +O%,( < +D4' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*9| %(+  0 p 5 (   x  c $ )% ``  %  XB  0D`f 0 0A?"`   2 <,% "`P E,$D  0 /The plot of kobs vs. [I] is essentially linear.j0    ~ 3 <\5%  @'( ,$ 0 :Should we just report kinact/Ki (i.e., slope) and be done?f; H  0޽h ? ̙335 - ___PPT10 +[D' 9% = @B D<' = @BA?%,( < +O%,( < +D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*2 %(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*2 D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*2 D' =%(D' =%(D@' =A@BB BB0B%(D' =1:Bvisible*o3>+B#style.visibility<*3 %(D' =-o6Bdissolve*<3<*3 +p+0+2 0 ++0+3 0 +  0     (   x  c $H% ``  %  XB  0D`X  0A?*  <K%   }%Schwartz, Kuzmic et al. (2014) Fig S5<&l 0   0 ,$D 0ZB  s *D|0 0 ZB  s *D|0@    <R% "`0 ?low [I]   <U% "`0 0   @high [I] +  <@Z%  [,$  0 !The initial slope depends on [I].N"l  p`-  p `-,$D 0   6`%  `- ?There must be a non-covalent complex formed during mixing time.J@     n2   0"`ppz  p`   0 z ,$D 0   6h%  ` hThis is a two-step mechanism0    n2   0"`ppFz  p`   0 z,$D 0F   6n%  ` LThe  linear kobs plot makes no sense.N'      n2   0"`ppH  0޽h ? ̙33___PPT10+}D5' v% = @B D' = @BA?%,( < +O%,( < +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?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<* 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 XP   (   x  c $% ``  %  XB  0D`  <|%   }%Schwartz, Kuzmic et al. (2014) Fig S6<&f  0A?"`'J  <d% "`0 . ^Error bars are standard error from triplicates: Initial rates are very well reproduced (10%).V_" +l  02  0 2,$D 0n2   0"`09   <% "` 2 /The problem with kinact is not in data quality.J0 z  0   0  7 ,$D 0n2   0"`0   <h% "`  j&The problem is with the fitting model.('H  0޽h ? ̙33 ___PPT10+-{D' p = @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<* +_ ! 0     (   x  c $% ``  %  XB  0D`  <d% d D<4___PPT9 kinact and Ki could not be determined, -the fit of averaged kobs values produced meaningless results for kinact and Ki -the data is good, but the reproducibility of kinact, Ki across replicates is very poor The diagnostic plot of kobs vs. [I] contradicts the plot of vi vs. [I] - kobs plot seems to suggest a single-step binding mechanism - vi plot (initial rates) strongly suggests a two-step mechanism j         %        1)/</y @`l     8  ,$D  0ZB   s *Dp     <( $ :  n6We can t use these results.   Bx( GQ Hv "`p@ ,$D 0 Y values were too large&H  0޽h ?  ̙33___PPT10+sDt' ( = @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 0 F(   x  c $% ``  (  XB  0D`  <%  \Why did the  classical algebraic method fail?//*  <% p@m D<4___PPT9 rInhibitor depletion Significant inhibition is seen at [Inhibitor] comparable with [Enzyme] Nonlinear control progress curve ([I] = 0) The nonlinearity is  slight but, as it happens, has a significant impact.  >J @`H  0޽h ? ̙33y___PPT10Y+D=' p = @B + " 0  2(   x  c $( ``  (  XB  0D`  <x(  q1. Change the assay: throw out this data and go back to the lab -linearity: can we find conditions where [S] >> KM? -tight binding: can we find conditions where [E] << [I]?/ ' + @`~  <?( P3  2. Change the method of data analysis: -use a differential equation model instead of simple algebra -that method makes no simplifying assumptions of any kindB% [ @`  < &( p  !3. Cross your fingers and hope for a meaningful result -use the traditional algebraic method anyway -this is the path of least resistance (no changes required)N8 L @`RB  @ s *DԔ  RB  s *DԔ P f  0"` H  0޽h ? ̙33y___PPT10Y+D=' p = @B +v $ 0 p x(   x  c $@( ``  (  XB  0D`l  6A1?"`P f  0"` 0fl  2@  2 ,$D 0t   6AjJ?"`0 2@n   0"`p `    <P(  4,$  0 NThis model is  integrated numerically .((  <dU(  t,$  0 HWhatever that means.H  0޽h ? ̙336.___PPT10+MyD' \( = @B D=' = @BA?%,( < +O%,( < +Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =+4 8?dCB0-#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<* 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   &(   x  c $d( ``  (  XB  0D`l  6A1?"`P f  0"` 0f  0A?"`@ l  6jJ"`-     <g(   d.DynaFit input  script :tl f f   ff,$D 0t   6jJ"` P  ZB  B s *DjJ     <Hm( f df dfixed constant:  rapid-equilibrium approximation &3#  <q(  g  :DynaFit script: ./published/Schw1473/Nera/06-global-R1.txt4;  + H  0޽h ? ̙335-___PPT10 +WD' p = @B D' = @BA?%,( < +O%,( < +D' =%(D' =%(D3' =4@BB BB%(D' =1:Bvisible*o3>+B#style.visibility<* %(D' =-o6Bdissolve*<3<* +) & 0  (   x  c ${( ``  (  XB  0D`f  0A?"`@@A  <}( D ,$ 0 p,global fit: all curves are analyzed together(- !H  0޽h ? ̙33___PPT10+2SDO' p = @B D ' = @BA?%,( < +O%,( < +DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* %(+8+0+ 0 +M ' 0     D (   x  c $( ``  (  XB  0D`l  6A>?"`N.  <( p,D LDynaFit output window:  <((   How do we get Ki out of this?H <  <8( : "B ,$ 0 Z We have chosen micromolar units throughout this analysis. Recall that kon was arbitrarily fixed at 100 M-1s-1 ( rapid equilibrium ) Recall that Ki is defined as koff/kon - *   >HIl2  6jJ"`r2'l @  @,$D  0   Bԩ( @  91Ki = koff/kon = 0.341 / 100 = 0.00341 M = 3.4 nM2   6"t2   6jJ"`` t2   6jJ"` H  0޽h ? ̙33A9___PPT10+.D' ( = @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 ^V ( (  ( x ( c $( ``  (  XB ( 0D` ( <(   }%Schwartz, Kuzmic et al. (2014) Fig S6<&f ( 0A?"` p _  ( <\( $ C, )Initial rate method: Ki = (4.0 0.5) nMz* ,d ( <( 0 p 8 .Global fit, Replicate #1: Ki = (3.4 0.1) nMz/ , ( C `A*data-model-t001-g001Data and model@ @  ( <l( p F }%Schwartz, Kuzmic et al. (2014) Fig S8<&# ( < ( p0,$  0 OSatisfactory agreement between results from two completely independent methods.PPH ( 0޽h ? ̙33___PPT10+;4K7D' ( = @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 +f / 0 N F 0  (  0 x 0 c $`( ``  (  XB 0 0D`  0 <( T@  Z(replicate #1 replicate #2 replicate #3))RB  0 s *D8c RB  0 s *D8c00 0 <T( 3@ Ki, nMJ$2 0 <D/   $1000 kinact, s-1d    0 </  h n*NUMERICAL method (differential equations):(+ " 0 < / `  U3.4 0.1 3.6 0.1 3.3 0.1 LB 0 c $D0 0  0 </ T a  [%0.86 0.05 0.85 0.05 0.96 0.07&& 0 <t/  ,$  0 CNotes: Three independent experiments (three separate 96-well plates run in sequence). Raw data and DynaFit scripts are distributed with the program. DynaFit script files: ./published/Schw1473/Nera/06-global-R1, -R2, -R3.txt Published results (PNAS, 2014) are very slightly different: concentrations were optimized.r<!W 6 \Df 0 0"`  0 <$/   Neratinib vs. EGFR double mutant$!   $ ' 0 <$)/ "`0:,$D  0 y)About 10% reproducibility plate to plate.4* H 0 0޽h ? ̙33  ___PPT10 +[D ' ,/ = @B D ' = @BA?%,( < +O%,( < +D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*0 %(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<*0 D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<*0 D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*0 %(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<*0 D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<*0 +p+0+0 0 ++0+0 0 +G 0 0 ia@8 (  8 x 8 c $?/ ``  /  XB 8 0D` 8 <?/ TJ  6replicate #1 replicate #2 replicate #3 average kobs073 2RB 8 s *D8cp RB 8 s *D8c00 8 <G/ 3@ Ki, nMJ$2 8 <O/ V  $1000 kinact, s-1d   ,  8 <8X/ h |ALGEBRAIC method ( Traditional Recipe )  using the same data:(? 6  8 <l]/ `a  *53 22 254 442 > 1 000 000 420 850++ LB  8 c $D p   8 <|b/ T| h  b,1.6 0.4 6.1 9.5 27 162000 10 19--f 8 0"`p  8 <g/   Neratinib vs. EGFR double mutant$!   $ RB 8 s *D8c  l d  8 d ,$D 0ZB 8  s *DԔP ` P ZB 8  s *DԔ P P ZB 8  s *DԔ 0 0 ZB 8  s *DԔ  ZB 8  s *DԔ` ZB 8  s *DԔ0 ` 0 TB 8  c $D` P ` TB 8  c $D` 0 ` TB 8  c $D`  ` TB 8 c $D  ` TB 8 c $D 0 ` TB 8 c $D P `  8  <o/  d  Ononsense values ( too large)H 8 0޽h ? ̙33~___PPT10^+kBFDB' p = @B D' = @BA?%,( < +O%,( < +D4' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<*8 %(+ 1 0 F>`!@ (  @ x @ c $y/ p  /   @ <z/ `  Bringing in differential equations can be expensive: -time to learn and train -money for new software Why not just stick with kinact/KI, like most people do? +   H @ 0޽h ? ̙33y___PPT10Y+D=' p = @B + 3 0 h ` \  (  \ x \ c $/ ``  /  XB \ 0D`f \ 0A?"`   \ </ F  'Schwartz, Kuzmic, et al. (2014) Fig S10<(  \ </ T ,$  0 CONCLUSIONS: Non-covalent initial binding is more important than chemical reactivity for the cellular potency of covalent anticancer drugs.NGf \ 0"` 0  \ <   dkinact(  \ < <   hKi0l D @  \ D @ ,$D 0 \  <U  E @  Lnon-covalent binding  \  <d D  Gchemical reactivity Dl   \  ,$D 0~B \ NDԔ0P0 ZB \  s *D@` @ZB \  s *D ~B \ NDԔ  l \ 6Ԕ"` ` pH \ 0޽h ? ̙33, $ ___PPT10 +>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 +  4 0 } d (  d x d c $/ ``  /  XB d 0D` d </ @ 'Schwartz, Kuzmic, et al. (2014) Fig S11<(f  d 0A?"`   d <l/ F1j ,$  0 HNon-covalent Kd vs. Cellular IC50 strong correlation for a larger panelvI & :H d 0޽h ? ̙33___PPT10+{D' / = @B DD' = @BA?%,( < +O%,( < +D{' =%(D#' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* d %(D' =+4 8?dCB1+#ppt_w/2BCB#ppt_xB*Y3>B ppt_x<* d D' =+4 8?\CB#ppt_yBCB#ppt_yB*Y3>B ppt_y<* d +8+0+ d 0 + 2 0    T t (  T x T c $0/ ``  /  XB T 0D` T <4 @6@ FThe traditional method to analyze covalent inhibition data breaks down if: - the  control progress curve ([I] = 0) is nonlinear - there is inhibitor depletion (i.e. when [E] is comparable with [I]) - or if both situations apply at the same time.<6 T </ "`|u,$D 0 LThe nonlinearity in the control curve ([I] = 0) can very  slight , by subjective standards, and yet the detrimental effect is profound."CE T <4 "`@z& ,$D 0 There is no need to redesign the assay to force the experimental data into conformity with the classic algebraic model. There is nothing  wrong with the data. It just cannot be analyzed in the usual way.2'QV T <p4 "` g ,$D 0 o=Instead one must use a differential equation model (DynaFit).>>l P   T  P,$D  0 T  <o P  Using this general numerical approach (DynaFit), we were able to measure the initial binding constants of covalent drugs and determine the impact of Kd on drug potency in cellular assays.M %TB  T  c $D  H T 0޽h ? ̙33C ; ___PPT10 +0%4DW ' '4 = @B D ' = @BA?%,( < +O%,( < +DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*T %(DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*T %(DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*T %(Dn' =%(D' =%(D' =4@BBBB%(D' =1:Bvisible*o3>+B#style.visibility<* T %(D' =+4 8?\CB#ppt_xBCB#ppt_xB*Y3>B ppt_x<* T D' =+4 8?dCB1+#ppt_h/2BCB#ppt_yB*Y3>B ppt_y<* T ++0+T 0 ++0+T 0 ++0+T 0 +  0 L :(  L x L c $414 `p  4  XB L 0D` L Z24  >?"6@ NNN?N0   Brion Murray  Pfizer Leader on the PNAS paper, and in other ways Art Wittwer  Confluence Technologies (formerly Pfizer) PK/PD initial scripts (and many other ideas) Phillip Schwartz  Takeda (formerly Pfizer) Data collection for EGFR inhibitors Jim Solowiej - Pfizer Data collection for EGFR inhibitors Y+ * -  & + ' 6u% T L Z44  >?"6@ NNN?N   "Questions ? 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