J. Am. Chem. Soc., 1997, 119(5), , DOI: /ja962780a

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J. Am. Chem. Soc., 1997, 119(5), 918-925, DOI:10.1021/ja962780a Terms & Conditions Electronic Supporting Information files are available without a subscription to ACS Web Editions. The American Chemical Society holds a copyright ownership interest in any copyrightable Supporting Information. Files available from the ACS website may be downloaded for personal use only. Users are not otherwise permitted to reproduce, republish, redistribute, or sell any Supporting Information from the ACS website, either in whole or in part, in either machinereadable form or any other form without permission from the American Chemical Society. For permission to reproduce, republish and redistribute this material, requesters must process their own requests via the RightsLink permission system. Information about how to use the RightsLink permission system can be found at http://pubs.acs.org/page/copyright/permissions.html Copyright 1997 American Chemical Society

Pseudo-Prolines (PPro) as a Molecular inge: Reversible Induction of Cis Amide Bonds into Peptide Backbones. Pascal Dumy, Michael Keller, Declan E. Ryan, Barbara Rohwedder, Torsten Wohr and Manfred Mutter. Contribution from the Institute of Organic Chemistry, University of Lausanne, BC-Dorigny, C- 1015, Lausanne, Switzerland. Spectra were recorded at 400 MI-Lz using a Bruker ARX spectrometer at 300 K. Samples of around 25 mg were dissolved in 0.4-0.5 ml of DMSOd 6. Chemical shifts were calibrated on the solvent isotopic impurity (2.49 ppm at 300 K). 2D experiments were typically acquired using 2K x 512 matrices over a 4000 z sweep width in both dimensions. Quadrature detection in the indirect dimension was achieved by using the TPPI procedurel. Scalar connectivities were recovered from 2D double quantum filtration (DQF) COSY experiments 2. Dipolar connectivities were obtained either through the conventional NOESY sequence 3 or the ROESY sequence 4 with mixing times from 150 to 200 ms. A randomization of the mixing length (± 5%) was introduced in the NOESY experiments in order to minimize coherence transfer. The spin lock mixing interval of the ROESY sequence was applied by coherent CW irradiation at yb 2 /2xr = 2 Kz. Experimental data processing was performed using the Felix software package 5. The standard sinebell squared routine was employed for apodization with a shift range of 60-900 and zero filling in both dimensions before 2D transformations were applied to end up with square matrices of 2K x 2K real point data. Complete proton resonance assignments were made using (DQF) COSY experiments, MQC was used to assign unambiguously the carbon resonances. J coupling constant were directly measured from highresolution ' -ID spectra (±0.1z) or simulated for complex or overlapped systems. Prochiral assignments for the 'Pro P and Me protons were achieved, in some cases, on the basis of relative interproton ROE intensities and J coupling constant values. 1 Drobny, G.; Pines, A., Sinton, S.; Wertekamp, D.; Wemmer, D. Faraday Div. Chem. Soc. Symp., 1979, 13, 48-58. 2 Piantini, V.; Sorensen, 0. W.; Ernst, R. R. J Am. Chem. Soc,. 1982, 104, 6800-680 1. 3 Jeener, J.; Meier, B..; Bachmann, P.; Ernst, R. R. J Chem. Phys., 1979, 71, 4546-4553. 4 Bothner-By, A. A.; Stephen, R. R-L.; Lee, J., Warren, C. D.; Jeanloz, R. W., J Am. Chem. Soc. 1984, 106, 811-813. 5 Biosym Technologies Inc., San Diego. Pseudo-Prolines (YPro) as a Molecular inge: Reversible Induction of Cis Amide Bonds into Peptide Backbones. Pascal Dumy, Michael Keller, Declan E. Ryan, Barbara Rohwedder, Torsten W6hr and Manfred Mutter.

Ac-Ala-Ser(MeMepro)N-Me (1) pros 0 Table 1. 1 NMR spectral parameters of compounds 1. N ('JN-a) a 3 a-p) ( 2 jp-p) 2-Me Ala 8.154 4.100 1.16(7.0) Ser(Yue~mepro) - 4.44(6. lpro-r) 4.17/4. 0 5 Pro-R( 8.8) 1.52/1. 4 3 pro-s NMe 8.176(4.5) 2.615 Ac 1.667 Table 2. 13 C NMR spectral parameters of compounds 1. O p 2-C 2-Me CO Ala 47.8 16.5 169.5 ser 59.2 67 90.5 25.2pro-s/22.4 169.2 Ac 21.8 Me 25.8 Pseudo-Prolines (TPro) as a Molecular inge: Reversible Induction of Cis Amide Bonds into Peptide Backbones. Pascal Dumy, Michael Keller, Declan E. Ryan, Barbara Rohwedder, Torsten Wohr and Manfred Mutter.

Ac-Ala-Thr(TMeMepro)N-Me (2) N Me 0 NMe Table 3. 1 NMR spectral parameters of compounds 2. N ( 3 JN-) c a-) ( 2 p-p-i) PMe 2-Me Ala 7.70 4.28 1.271(6.6) - Thr(Y M e* M epro) - 4.03(5.7) 4.12 1.29 1.52/1.50os NMe 8.6 2.61(3.6) Ac 1.805 Table 4. 13 NMR spectral parameters of compounds 2. OX 0 PMe C(2) 2-C CO Ala 46.8 18.5 169.7 Thr(" m ''"pro) 65.6 74.9 19.1 95.4 2 6. 1 8 pro-s/ 2 3. 9 168.9 Ac 22.2 168.2 Me 25.8 Pseudo-Prolines ('VPro) as a Molecular linge: Reversible Induction of Cis Anide Bonds into Peptide Backbones. Pascal Dumy, Michael Keller, Declan E. Ryan, Barbara Rohwedder, Torsten W6hr and Manfred Mutter.

Ac-Ala-Cys(TMeMepro)N-Me (3) pros Me N. 0 Table 5. 1 NMR spectral parameters of compounds 3. N ('JN-a) C3 ajo-o) 2 P-P) 2-Me Ala 8.21(6.9) 4.10 1.16 Cys(FueM'pro) - 5. 34 ( 6.4ro-R) 3. 6 2 pro-r/3. 2 0 (11.8) 1. 9 3 /1. 8 5 ro-s NMe 8.176(4.7) 2.85 Ac 1.667 Table 6. 1 NMR spectral parameters of compounds 3. a. 0 2-Me CO Ala 49.31 18.7 170.4 Cys(YMeMepro) 64.6 30.8 2 8. 9 pro-s/ 2 7. 6 171.2 Ac 22.5 168.2 Me 25.3 Pseudo-Prolines (TPro) as a Molecular inge: Reversible Induction of Cis Anide Bonds into Peptide Backbones. Pascal Dumy, Michael Keller, Declan E. Ryan, Barbara Rohwedder, Torsten W6hr and Manfred Mutter.

Ac-Ala-Ser(T,pro)N-Me (4) 0) pros N NMe Table 7. 1 NMR spectral parameters of compounds 4. N ( 3 JNl-ly) cc P ( 2 JfW.P{1) y 2- Ala 8.219(5.8) 4.29 1.18(6.90) - Ser(pro) - 4.31 4.09/3.83-5.17/4.96(3) Ser(Ypro) 4.48 4.18/4.03 4.88 Cis(28%) NMe 7.78(4.5) 2.57 NMe 8.13 2.60 Ac 1.81 Table 8. 13 C NMR spectral parameters of compounds 4. cx y 2-C CO Ala 46.8 16.6 169.2 Ser(YPpro) 59.2 69.7 78.5 169.2 Ser(PIlpro) Cis 59.8 71.2 79.1 Ac 21.9 168.9 Me 25.4(25.7) Pseudo-Prolines (TPro) as a Molecular inge: Reversible Induction of Cis Amide Bonds into Peptide Backbones. Pascal Duny, Michael Keller, Declan E. Ryan, Barbara Rohwedder, Torsten W~hr and Manfred Mutter.

Ac-Ala-Pro-N-Me (5) 0 pros N 0 NMe Table 9. 1 NMR spectral parameters of compounds 5. N ( 3 JN-o) X ( 3 Ja.-O) (2j P-P) y 5 Ala trans(82%) 8.05(7.5) 4.51 1.55(6.9) - - Pro trans - 4.2(3.8/8.4) 1. 9 7 P-'/1. 7 5 pro-r 1.88/1.86 3. 57 pro-r/3. 5 3 pro-s Ala Cis (18%) 7.99(7.3) 4.26 1.13(6.8) - - Pro Cis - 4.3(3.4/7.3) 2.04 1.76/1.68 3.38/3.36 Me trans 7.63 2.54(4.7) Me cis 7.94 2.58(4.7) Ac 1.79 Table 10. 13 C NMR spectral parameters of compounds 5. a p y 6 CO Ala trans 46.5 16.9 168.6 Pro trans 59.5 29.1 24.3 45.9 170.6 Ala Cis 46.7 17.5 168.7 Pro cis 50.6 31 21.6 46.2 170.9 Ac 22.1 171.8 Me 25.4 Me 25.7 Pseudo-Prolines ('PPro) as a Molecular inge: Reversible Induction of Cis Amide Bonds into Peptide Backbones. Pascal Dumy, Michael Keller, Declan E. Ryan. Barbara Rohwedder, Torsten Wahr and Manfred Mutter.

Succinyl-Val-Ser( pro)-phe-pna (7) Table 11. 1 NMR spectral parameters of compound 7 N('JN-a) cx (Jcc-P) 3 ( 2 Jp-a) Val 8.202(8.2) 3.94 1.89 Ser('F pro) 4.485 (7.3/ 5..0) 4.174pro-R 3.818 (8.7) Phe Succinyl (4-NO 2 )-Ph 8.417 (7.1) 2.42 10.53 4.637(5.4, 8.4) 8.2 (9.3) meta 3.07 2.96 (13.8,) 7.79 ortho 0.865(6.6) /0.855(6.6) 2-5.289 (3.7) 4.95 Pseudo-Prolines (TPPro) as a Molecular inge: Reversible Induction of Cis Anide Bonds into Peptide Backbones. Pascal Duny, Michael Keller. Declan E. Ryan, Barbara Rohwedder, Torsten W3hr and Manfred Mutter.

Succinyl-Val-Ser(Tm',mepro)-Phe-pNA (8) Table 12. 1 NMR spectral parameters of compound 8. N( JN-a) c. (3 Ja-P) P( 2JP-a) y 2-Me Ser(' MeMepro) - 4.64 (6.5,/1.9) 4. 10 2 pro-r 1.43 4.00 (9.1) Phe 8.46 (7.7) 4.702 3.2 -- Val 7.84 (8) 4.27 (6.2) 1.9 0.86 (6.8) 0.88 (6.8) Succinyl 2.45 (4-NO2)-Ph 10.68 8.2(9.3) meta 7.77 ortho Pseudo-Prolines ('TPro) as a Molecular linge: Reversible Induction of Cis Anide Bonds Into Peptide Backbones. Pascal Duny, Michael Keller, Declan E. Ryan, Barbara Rohwedder, Torsten W6hr and Manfred Mutter.

Succinyl-Val-Ser( Y(2-R),PM PrO)-Phe-pNA (9) Table 13. 1 NMR spectral parameters of compound 9 N( 3 JN-x) a ('Jcx-P) Val trans (90%) 8.159 (8.5) 3.885 (8.8) (2j J-P) 1.67 0.56 (6.6) /0.23 2- (6.7) Ser(W PMPpro) trans 4.65 (7.4/5.6) 4.122pro-R/4.005 6.396 (8.9) Val Cis (10%) 4.36 0.95 (6.5) Ser( PMP pro) cis 4.878 4.32 / 4.279 6.025 Phe trans 8.52 (7.2) 4.71 (5.9/8.4) 3.102 / 3.01 (14) Phe cis 8.888 (7.23) Succinyl 2.4 PMP 3.728(OMe) 6.98 (8.7) meta 7.71 ortho NO2Ph trans 10.639 8.2 (9.3) meta 7.8 ortho Table 14. 1 3 C NMR spectral parameters of compound 9. a. P y 2-C Val trans 55.6 29.25 17.9/19 - Ser(PW, pro) trans 58.3 67.3-89.7 Phe 55.0 37.1 Suc 29 29 - - PMP 55 (OMe) 113 meta 130 ortho (4-NO2)-Ph 124.7 meta 118.7 ortho Pseudo-Prolines ('PPro) as a Molecular inge: Reversible Induction of Cis Anide Bonds Into Peptide Backbones. Pascal Durny, Michael Keller, Declan E. Ryan, Barbara Rohwedder, Torsten Wahr and Manfred Mutter.

Succinyl-Val-Ser(W(2-S)PMPpro)-Phe-pNA (major) (10) Table 15. 1 NMR spectral parameters of compound 10. N ( 3 JN-a) a ( 3 Jc-O) 0(2JP-P) Val trans (50%) 7.53(8.9) 4.00 (8.3) 2.00 Ser(YPP trans ", pro) Val cis (50%) Ser(TPM., pro) cis Phe trans Phe cis Succinyl cis Succinyl trans PMP trans PMP cis (4-NO2)Ph trans (4-NO2)Ph cis - 4.704 (7.2/3.1) 7.65 (9.1) 4.44 (4.7/8.9) 4.853 (6.3,/1.9) 8.489 (7.2) 4.639 (5.7/8.7) 8.89 (7.5) 4.793 (7.0 /7.2) 2.39 2.33 2.22 2.08 3.73 (OMe) 6.9(8.5) meta 3.74 (OMe) 6.88(8.5) meta 10.49 8.21(9.3) meta 10.55 8.19(9.3) meta 3. 9 7 9 pror 3.864 (9.3) 2.064 4.29pro R 4.02 (8.9) 3.076 (13.8), 2.977 3.175 (14), 3.108 7.26 ortho 7.29 ortho 7.8 ortho 7.77 ortho y 0.79(6.6)0.7 44(6.8) 0.82 (6.6), 0.69 (6.8) 2-6.32 6.17 Table 16. 13 C NMR spectral parameters of compound 10. Val trans a 54.7 0 y 29 19.1/16.8 2-C Ser( PMP, pro) trans 58.2 66.62 88.7 Phe trans 55.2 37.105 Val cis 54.66 28.97 19.1/16.6 Ser(Tp'l", pro) cis 58.18 69.9 90.0 Phe cis 54.3 37.1 Suc 28.2 28.2 - NO2PhN 124.7 meta 118.7 meta PMP 54.7 (OMe) 127.9 meta 119.3 ortho Pseudo-Prolines ('Pro) as a Molecular inge: Reversible Induction of Cis Anide Bonds into Peptide Backbones. Pascal Dumy, Michael Keller, Declan E. Ryan, Barbara Rohwedder, Torsten W6hr and Manfred Mutter.

L) - Y *, 111 Ac-Ala-Ser['P Mo 101 to 115 Kcal.morl am 116 to 130 Kcal.mor 131 to 145 Kcal.molpro]-NMe 180 Trans conformation E=20.1Kcal.mol' Cis conformation E=19.9 Kcal.mol' -1801-180 180-180 180 mm 101 to 115 Kcal.mol 116 to 130 Kcal.mol... 131 to 145 Kcal.mol

-~-~ j Trans conformation E=27.5 Kcal. mot' Ac-Ala-Pro-NMe 180 Cis conformation E=29.9 Kcal.mo' I Pt -18-180 180-180 180 m 81 to 95 Kcal.mol) 96 to 110 Kcal.mol" Ill to 125 Kcal.mol m 83 to 97 Kcal.mol 98 to 112 Kcal.niol, 113 to 127 Kcal.mol"

II -~ Ii Ac-Ala-Ser[P MeMe pro]-nme Trans conformation E= -44.9 Kcal.mor' Cis conformation E= -48.0 Kcal.mot C) ac 5 4 00 oo 00-180 180-47 to 61 Kcal.mol - 62 to 76 Kcal.mol' 77 to 91 Kcal.mol- - 32 to 46 Kcal.mol" - 47 to 61 Kcal.mol 62 to 76 Kcal.mol

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