Stabilisation of a short α-helical VIP fragment by side chain to side chain cyclisation: A comparison of common cyclisation motifs by circular dichroism

Journal of Peptide Science

Volumn 19, Issue 7, 2013, Pages 423-432

  Frankiewicz, Lukasz ^a   Betti, Cecilia ^a   Guillemyn, Karel ^a   Tourwé, Dirk ^a   Jacquot, Yves ^b   Ballet, Steven ^a  

^a VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^b Centre National de la Recherche Scientifique   (France)

Author keywords

Circular dichroism; Cyclisation motifs; Helix stabilisation; Huisgen cycloaddition; Macrolactamisation; Ring closing metathesis

Indexed keywords

ALKYNE; AZIDE; CYCLOPEPTIDE; PEPTIDE FRAGMENT; TRIAZOLE; VASOACTIVE INTESTINAL POLYPEPTIDE;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; CYCLIZATION; CYCLOADDITION; HUMAN; PRECURSOR; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN CROSS LINKING; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; RING CLOSING METATHESIS; CHEMISTRY; COMPARATIVE STUDY; PROTEIN STABILITY; SYNTHESIS;

CIRCULAR DICHROISM; CYCLIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; VASOACTIVE INTESTINAL PEPTIDE;

EID: 84878972564     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.2515     Document Type: Article

References (40)

1. Guharoy M, Chakrabarti P. Secundary structure based analysis and classification of biological interfaces: identification of binding motifs in protein-protein interactions. Bioinformatics 2007; 23: 1909-1918. DOI: 10.1093/bioinformatics/btm274
2. Guharoy M, Chakrabarti P. Empirical estimation of the energetic contribution of individual interface residues in structures of protein-protein complexes. J. Comput. Aided Mol. Des. 2009; 23(9): 645-654. DOI: 10.1007/s10822-009-9282-3
3. Vlieghe P, Lisowski V, Martinez J, Khrestchatisky M. Synthetic therapeutic peptides: science and market. Drug Discov. Today 2010; 15: 40-56. DOI: 10.1016/j.drudis.2009.10.009
4. Katsara M, Tselios T, Deraos S, Deraos G, Matsoukas MT, Lazoura E, Matsoukas J, Apostopoulos V. Round and round we go: cyclic peptides in disease. Curr. Med. Chem. 2006; 13: 2221-2232. DOI:10.2174/092986706777935113
5. White CJ, Yudin AK. Contemporary strategies for peptide macrocyclization. Nature Chem. 2011; 3: 509-524. DOI: 10.1038/nchem.1062
6. Driggers EM, Hale SP, Lee J, Terret NK. Macrocycles for drug discovery. An underexploited structural class. Nature Rev. Drug. Disc. 2008; 7: 608-624. DOI: 10.1038/nrd2590
7. Kelso MJ, Hoang HN, Oliver WV, Sokolenko N, March DR, Appleton TG, Fairlie DP. A cyclic metallopeptide induce alpha helicity in short peptide fragments of thermolysin. Angew. Chem. Int. Ed. 2003; 42: 421-424. DOI: 10.1002/anie.200390128
8. Garner J, Harding MM. Design and synthesis of α-helical peptides and mimetics. Org. Biomol. Chem. 2007; 5: 3577-3585. DOI: 10.1039/B710425A
9. Davis JM, Tsou LK, Hamilton AD. Synthetic non-peptide mimetics of α-helices. Chem. Soc. Rev. 2007; 36: 326-334. DOI: 10.1039/B608043J
10. Walensky LD, Kung AL, Escher I, Malia TJ, Barbuto S, Wright RD, Wagner G, Verdine GL, Korsmeyer SJ. Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 Helix. Science 2004; 305: 1466-1470. DOI: 10.1126/science.1099191
11. Verdine GL, Hilinski GJ. Stapled peptides for intracellular drug targets. Meth. Enzymol. 2012; 503: 3-33. DOI: 10.1016/B978-0-12-396962-0.00001-X
12. I-catalyzed azide-alkyne intramolecular i-to-(i+4) side-chain-to-side-chain cyclization promotes the formation of helix-like secondary structures. Eur. J. Org. Chem. 2010; 446-457. DOI: 10.1002/ejoc.200901157
13. Yoshida M, Mori A, Kotani E, Oka M, Makino H, Fujita H, Ban J, Ikeda Y, Kawamoto T, Goto M, Kimura H, Baba A, Yasuma T. Discovery of novel and potent orally active calcium-sensing receptor antagonists that stimulate pulselike parathyroid hormone secretion: synthesis and structure-activity relationships of tetrahydropyrazolopyrimidine derivatives. J. Med. Chem. 2011; 54: 1430-1440. DOI: 10.1021/jm101452x
14. Kawamoto SA, Coleska A, Ran X, Yi H, Yang CY, Wang S. Design of triazole-stapled BCL9 α-helical peptides to target the β-Catenin/B-Cell CLL/lymphoma 9 (BCL9) protein-protein interaction. J. Med. Chem. 2012; 55: 1137-1146. DOI: 10.1021/jm201125d
15. Harrison RS, Ruiz-Gómez G, Hill TA, Chow SY, Shepherd NE, Lohman RJ, Abbenante G, Hoang HN, Fairlie DP. Novel helix-constrained nociceptin derivatives are potent agonists and antagonists of ERK phosphorylation and thermal analgesia in mice. J. Med. Chem. 2010; 53:8400-8408. DOI: 10.1021/jm101139f
16. Blackwell HE, Grubbs RH. Highly efficient synthesis of covalently cross-linked peptide helices by ring-closing metathesis. Angew. Chem. Int. Ed. 1998; 37: 3281-3284. DOI: 10.1002/(SICI)1521-3773(19981217)37:23<3281::AID-ANIE3281>3.0.CO;2-V
17. Schafmeister CE, Po J, Verdine GL. An all-hydrocarbon cross-linking system for enhancing the helicity and metabolic stability of Peptides. J. Am. Chem. Soc. 2000; 122: 5891-5892. DOI: 10.1021/ja000563a
18. Onoue S, Matsumoto A, Nagano Y, Ohshima K, Ohmori Y, Yamada S, Kimura R, Yajima T, Kashimoto K. α-Helical structure in the C-terminus of vasoactive intestinal peptide: functional and structural consequences. Eur. J. Pharmacol.. 2004; 485: 307-316. DOI: 10.1016/j.ejphar.2003.11.046 Nicole P, Lins L, Rouyer-Fessard C, Drouot C, Fulcrand P, Thomas A, Couvineau A, Martinez J, Brasseur R, Laburthe M. Identifiaction of key residues for interaction of vasoactive intestinal peptide with human VPAC1 and VPAC2 receptors and development of a highly selective VPAC1 receptor agonist. J. Biol. Chem. 2000; 275: 24003-24012. DOI:10.1074/jbc.M002325200
19. Larregola M, Lequin O, Karoyan P, Guianvarc'h D, Lavielle S. β-Amino acids containing peptides and click-cyclized peptide as β-turn mimics: a comparative study with 'conventional' lactam- and disulfide-bridged hexapeptides. J. Pept. Sci. 2011; 17: 632-643. DOI: 10.1002/psc.1382
20. Seebach D, Gardiner J. β-Peptidic peptidomimetics. Acc. Chem. Res. 2008; 41: 1366-1375. DOI: 10.1021/ar700263g
21. Cammers-Goodwin A, Allen TJ, Oslick SL, McClure KF, Lee JH, Kemp DS. Mechanism of stabilization of helical conformations of polypeptides by water containing trifluoroethanol. J. Am. Chem. Soc. 1996; 118: 3082-3090. DOI: 10.1021/ja952900z
22. Luo P, Baldwin RL. Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry 1997; 36: 8413-8421. DOI: 10.1021/bi9707133
23. Skwierawska A, Oldziej S, Liwo A, Scheraga HA. Conformational studies of the C-terminal 16-amino-acid-residue fragment of the B3 domain of the immunoglobulin binding protein G from streptococcus. Biopolymers 2009; 91: 37-51. DOI: 10.1002/bip.21080
24. Jasanoff A, Fersht AR. Quantitative determination of helical propensities from trifluoroethanol titration curves. Biochemistry 1994; 33: 2129-2135. DOI: 10.1021/bi00174a020
25. Woody RW. Studies of theoretical circular dichroism of polypeptides: contributions of beta-turns. Peptides, Polypeptides and Proteins, Blout ER, Bovey FA, Goodman M and Lotan N (Eds). New-York: John Wiley & Sons, 1974; 338-350.
26. Platt JR. Classification of spectra of cata-condensed hydrocarbons. J. Chem. Phys. 1949; 17: 484-495. DOI: 10.1063/1.1747293
27. Klevens HB, Platt JR. Spectral resemblances of cata-condensed hydrocarbons. J. Chem. Phys. 1949; 17: 470-481. DOI: 10.1063/1.1747291
28. Wollmer A, Fleischhauer J, Strassburger W, Thiele H, Brandenburg D, Dodson G, Mercola D. Side-chain mobility and the calculation of tyrosyl circular dichroism of proteins. Implications of a test with insulin and des-B1-phenylalanine insulin. Biophys. J. 1977; 20: 233-243. DOI:10.1016/S0006-3495(77)85546-X
29. Woody RW, Dunker AK. Aromatic and cystine side-chain circular dichroism in proteins. Circular Dichroism and the Conformational Analysis of Biomolecules, Fasman GD (Eds). New York and London: Plenum, 1996; 109-157.
30. Vijayakumar EKS, Balaram P. Stereochemistry of α-aminoisobutyric acid peptides in solution: helical conformations of protected decapeptides with repeating Aib-L-Ala and Aib-L-val sequences. Biopolymers 1983; 22: 2133-2140. DOI: 10.1002/bip.360220911
31. 10 versus α-helix: a molecular dynamics study of the conformational preferences of Aib and alanine. J. Am. Chem. Soc. 1994; 116: 11915-11921. DOI: 10.1021/ja00105a034
32. Raghothama S, Chaddha M, Balaram P. Determination of Aib residue conformation in peptides using diagnostic sidechain-backbone nuclear Overhauser effects. Proc. Natl. Acad. Sci. India 1996; 66: 33-44
33. Manning MC, Woody RW. Theoretical CD studies of polypeptides helices: examination of important electronic and geometric factors. Biopolymers 1991; 31: 569-586. DOI: 10.1002/bip.360310511
34. 10-/α-helix equilibrium in synthetic peptides. J. Pept. Res. 2001; 58: 108-116. DOI: 10.1034/j.1399-3011.2001.00858.x
35. 10-helix. J. Am. Chem. Soc. 1996; 118: 2744-2745. DOI: 10.1021/ja9537383
36. Blackwell HE, Sadowsky JD, Howard RJ, Sampson JN, Chao JA, Steinmetz WE, O'Leary DJ, Grubbs RH. Ring-closing metathesis of olefinic peptides: design, synthesis, and structural characterization of macrocyclic helical peptides. J. Org. Chem. 2001; 66: 5291-5302. DOI: 10.1021/jo015533k
37. Sharma GVM, Yadav TA, Choudhary M, Kunwar AC. Design of β-amino acid with backbone-side chain interactions: stabilization of 14/15 helix in α/β-peptides. J. Org. Chem. 2012; 77: 6834-6848. DOI: 10.1021/jo300865d
38. Hayen A, Schmitt MA, Ngassa FN, Thomasson KA, Gellman SH. Two helical conformations from a single foldamer backbone: "split personality" in short α/β-peptides. Angew. Chem. Int. Ed. 2004; 43: 505-510. DOI: 10.1002/anie.200352125
39. 10-/α-helix transition: critical main-chain length. Biopolymers Pept. Sci. 2008; 90: 567-574. DOI: 10.1002/bip.21016
40. Caporale A, Sturlese M, Gesiot L, Zanta F, Wittelsberger A, Cabrelle C. Side Chain cyclization based on serine residues: synthesis, structure, and activity of a novel cyclic analogue of the parathyroid hormone fragment1-11. J. Med. Chem. 2010; 53: 8072-8079. DOI: 10.1021/jm1008264