Privileged scaffolds targeting reverse-turn and helix recognition

Expert Opinion on Therapeutic Targets

Volumn 12, Issue 1, 2008, Pages 101-114

  Che, Ye ^a   Marshall, Garland R ^a  

^a WASHINGTON UNIVERSITY   (United States)

Author keywords

Drug discovery; Helix; Interaction; Privileged structure; Protein protein reverse turn

Indexed keywords

ASPERLICIN; BENZODIAZEPINE; CHOLECYSTOKININ RECEPTOR BLOCKING AGENT; MANGANESEDICHLORO(3,10,13,20,26 PENTAAZATETRACYCLO[20.3.1.0(4,9).0(14,19)] 1(26),22(23),24 HEXACOSATRIENE); METAL; PROTEIN FARNESYLTRANSFERASE INHIBITOR; RNA DIRECTED DNA POLYMERASE INHIBITOR;

ALPHA HELIX; BETA SHEET; BINDING AFFINITY; CHEMICAL MODIFICATION; CLINICAL TRIAL; COMBINATORIAL CHEMISTRY; COMPLEX FORMATION; DRUG DESIGN; DRUG RESEARCH; DRUG STRUCTURE; DRUG TARGETING; ENTROPY; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; MOLECULAR INTERACTION; MOLECULAR MIMICRY; MOLECULAR RECOGNITION; NONHUMAN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; STRUCTURE ACTIVITY RELATION;

ANIMALS; BINDING SITES; CYTOSKELETAL PROTEINS; DRUG DESIGN; HUMANS; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, SECONDARY; SURFACE PROPERTIES;

EID: 39049124587     PISSN: 14728222     EISSN: None     Source Type: Journal    
DOI: 10.1517/14728222.12.1.101     Document Type: Review

References (158)

1. Che Y. Protein-protein recognition: structure, energetics and drug design. Ph.D. Thesis, St. Louis, MO: Washington University 2003
2. Toogood PL. Inhibition of protein-protein association by small molecules: Approaches and progress. J Med Chem 2002;45:1543-58
3. Berg T. Modulation of protein-protein interactions with small organic molecules. Angew Chem-Int Edit 2003;42:2462-81
4. Arkin MR, Wells JA. Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov 2004;3:301-17
5. Yin H, Hamilton AD. Strategies for targeting protein-protein interactions with synthetic agents. Angew Chem Int Ed 2005;44:4130-63
6. Che Y, Brooks BR, Marshall GR. Development of small molecules designed to modulate protein-protein interactions. J Comput Aided Mol Des 2006;20:109-30
7. Lipinski CA, Lombardo F, Dominy BW, Feeney PJ. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv Drug Deliv Rev 2001;46:3-26
8. Wright PE, Dyson HJ. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 1999;293:321-31
9. Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 2005;6:197-208
10. Dunker AK, Brown CJ, Lawson JD, et al. Intrinsic disorder and protein function. Biochemistry 2002;41:6573-82
11. Radivojac P, Obradovic Z, Smith DK, et al. Protein flexibility and intrinsic disorder. Protein Sci 2004;13:71-80
12. Radivojac P, Iakoucheva LM, Oldfield CJ, et al. Intrinsic disorder and functional proteomics. Biophys J 2007;92:1439-56
13. Uversky VN. Natively unfolded proteins: a point where biology waits for physics. Protein Sci 2002;11:739-56
14. Tompa P. Intrinsically unstructured proteins. Trends Biochem Sci 2002;27:527-33
15. Tampa P. The functional benefits of protein disorder. J Mol Struct-Theochem 2003;666:361-71
16. Meszaros B, Tompa P, Simon I, Dosztanyi Z. Molecular principles of the interactions of disordered proteins. J Mol Biol 2007;372:549-61
17. Iakoucheva LM, Brown CJ, Lawson JD, et al. Intrinsic disorder in cell-signaling and cancer-associated proteins. J Mol Biol 2002;323:573-84
18. Cheng YG, LeGall T, Oldfield CJ, et al. Abundance of intrinsic disorder in protein associated with cardiovascular disease. Biochemistry 2006;45:10448-60
19. Walsh CT. Posttranslational Modification of Proteins: Expanding Nature's Inventory. Greenwood Village, CO: Roberts and Co. Publishers, 2005
20. Walsh CT, Garneau-Tsodikova S, Gatto GJ. Protein posttranslational modifications: the chemistry of proteome diversifications. Angew Chem Int Ed 2005;44:7342-72
21. Mohan A, Oldfield CJ, Radivojac P, et al. Analysis of molecular recognition features (MoRFs). J Mol Biol 2006;362:1043-59
22. Mammen M, Shakhnovich EI, Whitesides GM. Using a convenient, quantitative model for torsional entropy to establish qualitative trends for molecular processes that restrict conformational freedom. J Org Chem 1998;63:3168-75
23. Marshall GR, Head RD, Ragno R. Affinity Prediction: The Sina Qua Non. In: Thermodynamics in Biology. Di Cera E, editor. Oxford: OUP 2000; p. 87-111
24. Cheng Y, LeGall T, Oldfield CJ, et al. Rational drug design via intrinsically disordered protein. Trends Biotechnol 2006;24:435-42
25. du Vigneaud V, Ressler C, Swan CJM, et al. The synthesis of an octapeptide amide with the hormonal activity of oxytocin. J Am Chem Soc 1953;75:4879-80
26. Sewald N, Jakubke H-D. Peptides: Chemistry and Biology. Weinheim, Germany: Wiley-VCH, 2002
27. Marshall GR. A hierarchical approach to peptidomimetic design. Tetrahedron 1993;49:3547-58
28. Pelton JT, Gulya K, Hruby VJ, et al. Conformationally restricted analogs of somatostatin with high μ-opiate receptor specificity. Proc Natl Acad Sci USA 1985;82:236-9
29. Bauer W, Briner U, Doepfner W, et al. Sins 201-995 - a very potent and selective octapeptide analog of somatostatin with prolonged action. Life Sci 1982;31:1133-40
30. Evans BE, Rittle KE, Bock MG, et al. Methods for drug discovery - development of potent, selective, orally effective cholecystokinin antagonists. J Med Chem 1988;31:2235-46
31. Rose GD, Gierasch LM, Smith JA. Turns in peptides and proteins. Adv Prot Chin 1985;37:1-109
32. Marshall GR. Three-dimensional structure of peptide-protein complexes: implications for recognition. Curr Opin Struct Biol 1992;2:904-19
33. Marshall GR. Peptide interactions with G-protein coupled receptors. Biopolymers 2001;60:246-77
34. Tyndall JDA, Pfeiffer B, Abbenante C, Fairlie DP. Over one hundred peptide-activated G protein-coupled receptors recognize ligands with turn structure. Chem Rev 2005;105:793-826
35. Ripka WC, Delucca GV, Bach AC, et al. Protein β-turn mimetics. 1. Design, synthesis, and evaluation in model cyclic-peptides. Tetrahedron 1993;49:3593-608
36. Hata M, Marshall GR. Do benzodiazepines mimic reverse-turn structures? J Comput Aided Mol Des 2006;20:321-31
37. Chang RSL, Lotti VJ, Monaghan RL, et al. A potent nonpeptide cholecystokinin antagonist selective for peripheral-tissues isolated from aspergillus-alliaceus. Science 1985;230:177-9
38. Evans BE, Bock MG, Rittle KE, et al. Design of potent, orally effective, nonpeptidal antagonists of the peptide-hormone cholecystokinin. Proc Natl Acad Sci USA 1986;83:4918-22
39. Blackburn BK, Lee A, Baier M, et al. From peptide to non-peptide. 3. Atropisomeric GPIIbIIIa antagonists containing the 3,4-dihydro-1H-1,4-benzodiazepine-2,5-dione nucleus. J Med Chem 1997;40:717-29
40. Shigeri Y, Ishikawa M, Ishihara Y, Fujimoto M. A potent nonpeptide neuropeptide Y Y1 receptor antagonist, a benzodiazepine derivative. Life Sci 1998;63:PL151-PL160
41. Dziadulewicz EK, Brown MC, Dunstan AR, et al. The design of non-peptide human Bradykinin B-12 receptor antagonists employing the benzodiazepine peptidomimetic scaffold. Bioorg Med Chem Lett 1999;9:463-8
42. Haskell-Luevano C, Rosenquist A, Sauces A, et al. Compounds that activate the mouse melanocortin-1 receptor identified by screening a small molecule library based upon the beta-turn. J Med Chem 1999;42:4380-7
43. Miller WH, Alberta DP, Bhatnagar PK, et al. Discovery of orally active nonpeptide vitronectin receptor antagonists based on a 2-benzazepine Gly-Asp mimetic. J Med Chem 2000;43:22-6
44. Patchett AA, Nargund RP. Privileged structures - an update. Ann Rep Med Chem 2000;35:269-98
45. Hirschmann R, Nicolaou KC, Pietranico S, et al. Nonpeptidal peptidomimetics with a β-D-glucose scaffolding - a partial somatostatin agonist bearing a dose structural relationship to a potent, selective substance-P antagonist. J Am Chem Soc 1992;114:9217-18
46. Hirschmann R, Nicolaou KC, Pietranico S, et al. De-nova design and synthesis of somatostatin nonpeptide peptidomimetics utilizing β-D-glucose as a novel scaffolding. J Am Chem Soc 1993;115:12550-68
47. Hirschmann R, Hynes J, Cichy-Knight MA, et al. Modulation of receptor and receptor subtype affinities using diastereomeric and enantiomeric monosaccharide scaffolds as a means to structural and biological diversity. A new route to ether synthesis. J Med Chem 1998;41:1382-91
48. 1 integrin antagonists based on β-D-mannose as rigid scaffold. Angew Chem-Int Edit 2001;40:3870-3
49. Hanessian S, Moitessier N, Wilmouth S. Tetrahydrofuran as a scaffold for peptidomimetics. Application to the design and synthesis of conformationally constrained metalloproteinase inhibitors. Tetrahedron 2000;56:7643-60
50. Ghosh M, Dulina RG, Kakarla R, Sofia MJ. Efficient synthesis of a stereochemically defined carbohydrate scaffold: Carboxymethyl 2-acetamido-6-azido-4-O-benzyl-2-deoxy-α-D-glucopyranoside. J Org Chem 2000;65:8387-90
51. Schweizer F. Glycosamino acids: building blocks for combinatorial synthesis - implications for drug discovery. Angew Chem-Int Edit 2001;41:230-53
52. Gruner SAW, Locardi E, Lohof E, Kessler H. Carbohydrate-based mimetics in drug design: sugar amino acids and carbohydrate scaffolds. Chem Rev 2002;102:491-514
53. Peri F, Cipolla L, Forni E, Nicotra F. Carbohydrate-based scaffolds for the generation of sortiments of bioactive compounds. Monatsh Chem 2002;133:369-82
54. Le GT, Abbenante G, Becker B, et al. Molecular diversity through sugar scaffolds, Drug Discov Today 2003;8:701-9
55. Jensen KJ, Brask J. Carbohydrates in peptide and protein design. Biopolymers 2005;80:747-61
56. Freidinger RM, Veber DF, Perlow DS, et al. Bioactive conformation of luteinizing-hormone-releasing hormone - evidence from a conformationally constrained analog. Science 1980;210:656-8
57. Nagai U, Sato K, Nakamura R, Kato R. Bicyclic turned dipeptide (BTD) as a β-turn mimetic - its design, synthesis and incorporation into bioactive peptides. Tetrahedron 1993;49:3577-92
58. Hanessian S, McNaughtonSmith G, Lombart HG, Lubell WD. Design and synthesis of conformationally constrained amino acids as versatile scaffolds and peptide mimetics. Tetrahedron 1997;53:12789-854
59. Halab L, Gosselin F, Lubell WD. Design, synthesis, and conformational analysis of azacycloalkane amino acids as conformationally constrained probes for mimicry of peptide secondary structures. Biopolymers 2000;55:101-22
60. Belvisi L, Colombo L, Manzoni L, et al. Design, synthesis, conformational analysis and application of azabicycloalkane amino acids as constrained dipeptide mimics. Synlett 2004;1149-71
61. Cluzeau J, Lubell WD. Design, synthesis, and application of azabicyclo[XYO] alkanone amino acids as constrained dipeptide surrogates and peptide mimics. Biopolymers 2005;80:98-150
62. Hinds MG, Welsh JH, Brennand DM, et al. Synthesis, conformational properties, and antibody recognition of peptides containing β-turn mimetics based on α-alkylproline derivatives. J Med Chem 1991; 34:1777-89
63. Genin MJ, Johnson RL. Design, synthesis, and conformational-analysis of a novel spiro-bicyclic system as a type-II β-turn peptidomimetic. J Am Chem Soc 1992;114:8778-83
64. Chalmers DK, Marshall GR. Pro-D-NMe-amino acid and D-Pro-NMe-amino acid - simple, efficient reverse-turn constraints. J Am Chem Soc 1995;117:5927-37
65. Takeuchi Y, Marshall GR. Conformational analysis of reverse-turn constraints by N-methylation and N-hydroxylation of amide bonds in peptides and non-peptide mimetics. J Am Chem Soc 1998;120:5363-72
66. Chung YJ, Christianson LA, Stanger HE, et al. A β-peptide reverse turn that promotes hairpin formation. J Am Chem Soc 1998;120:10555-6
67. Chung YJ, Huck BR, Christianson LA, et al. Stereochemical control of hairpin formation in β-peptides containing dinipecotic acid reverse turn segments. J Am Chem Soc 2000;122:3995-4004
68. Smith AB, Wang WY, Sprengeler PA, Hirschmann R. Design, synthesis, and solution structure of a pyrrolinone-based β-turn peptidomimetic. J Am Chem Soc 2000;122:11037-8
69. 3 integrin for a new cancer therapy. Angew Chem-Int Edit 1997;36:1375-89
70. 3 integrin inhibitor cyclo(-RGDfV-) and its retro-inverso peptide. J Am Chem Soc 1997;119:1328-35
71. 3 integrin antagonists. J Med Chem 1999;42:3033-40
72. 7 integrin antagonists. J Med Chem 2001;44:2586-92
73. 3 integrins. J Med Chem 2002;45:1045-51
74. 3 integrin antagonists. J Med Chem 2001;44:1938-50
75. Fujii N, Oishi S, Hiramatsu K, et al. Molecular-size reduction of a potent CXCR4-chemokine antagonist using orthogonal combination of conformation- and sequence-based libraries. Angew Chem-Int Edit 2003;42:3251-3
76. Porcelli M, Casu M, Lai A, et al. Cyclic pentapeptides of chiral sequence DLDDL as scaffold for antagonism of G-protein coupled receptors: synthesis, activity and conformational analysis by NMR and molecular dynamics of ITF 1565 a substance P inhibitor. Biopolymers 1999;50:211-19
77. Nikiforovich GV, Kover KE, Zhang WJ, Marshall GE. Cyclopentapeptides as flexible conformational templates. J Am Chem Soc 2000;122:3262-73
78. Che Y, Marshall GR. Engineering cyclic tetrapeptides containing chimeric amino acids as preferred reverse-turn scaffolds. J Med Chem 2006;111-24
79. Tian ZQ, Bartlett PA. Metal coordination as a method for templating peptide conformation. J Am Chem Soc 1996;118:943-9
80. Shi Y, Sharma S. Metallopeptide approach to the design of biologically active ligands: design of specific human neutrophil elastase inhibitors. Bioorg Med Chem Lett 1999;9:1469-74
81. Shi Y, Cai H-Z, Yang WH, et al. Conformationally constrained metallopeptide template for melanocortin-1 receptor. New Orleans, LA: 218th ACS National Meeting, 1999
82. Marshall GR. From Merrifield to MetaPhore: a random walk with serendipity. San Diego, CA Peptides: The Wave of the Future. Proceedings of 17th American Peptide Symposium, 2001
83. Zhang W-J, Wu Y, Gao Y, et al. Metal-pentaazacrown peptidomimetics: RGD and WRY. Boston, MA: Peptide Revolution: Genomics, Proteomics & Therapeutics. Proceedings of the 18th American Peptide Symposium, 2003
84. Reaka AJ, Ho CM, Marshall GR. Metal complexes of chiral pentaazacrowns as conformational templates for β-turn recognition. J Comput Aided Mol Des 2002;16:585-600
85. Che Y, Brooks BR, Riley DP, et al. Engineering metal complexes of chiral pentaazacrowns as privileged reverse-turn scaffolds. Chem Biol Drug Des 2007;69:99-110
86. Aston KW, Henke SL, Modak AS, et al. Asymmetric-synthesis of highly functionalized polyazamacrocycles via reduction of cyclic peptide precursors. Tetrahedron Len 1994;35:3687-90
87. Riley DP, Weiss RH. Manganese macrocyclic ligand complexes as mimics of superoxide-dismutase. J Am Chem Soc 1994;116:387-8
88. Riley DP, Henke SL, Lennon PJ, et al. Synthesis, characterization, and stability of manganese(II) C-substituted 1,4,7,10,13-pentaazacyclopentadecane complexes exhibiting superoxide dismutase activity. Inorg Chem 1996;35:5213-31
89. Riley DP, Lennon PJ, Neumann WL, Weiss RH. Toward the rational design of superoxide dismutase mimics: mechanistic studies for the elucidation of substituent effects on the catalytic activity of macrocyclic manganese(II) complexes. J Am Chem Soc 1997;119:6522-8
90. Salvemini D, Wang ZQ, Zweier JL, et al. A nonpeptidyl mimic of superoxide dismutase with therapeutic activity in rats. Science 1999;286:304-6
91. Riley DP. Functional mimics of superoxide dismutase enzymes as therapeutic agents. Chem Rev 1999;99:2573-87
92. Aston K, Rath N, Naik A, et al. Computer-aided design (CAD) of Mn(II) complexes: superoxide diamutase mimetics with catalytic activity exceeding the native enzyme. Inorg Chem 2001;40:1779-89
93. Salvemini D, Riley DP, Cuzzocrea S. SOD mimetics are coming of age. Nat Rev Drug Discov 2002;1:367-74
94. Macarthur H, Westfall TC, Riley DR et al. Inactivation of catecholamines by superoxide gives new insights on the pathogenesis of septic shock. Proc Natl Acad Sci USA 2000;97:9753-8
95. Samlowski WE, Petersen R, Cuzzocrea S, et al. A nonpeptidyl mimic of superoxide dismutase, M40403, inhibits dose-limiting hypotension associated with interleukin-2 and increases its antitumor effects. Nat Med 2003;9:750-5
96. Aquaro S, Muscoli C, Pollicita M, et al. Selective removal of superoxide anions is crucial for HIV replication in human primary macrophages and prevents peroxynitrite mediated apoptosis in neurons. Antiviral Res 2005;65:A28-A28
97. Tamamura H, Otaka A, Murakami T, et al. An anti-HIV peptide, T22, forms a highly active complex with Zn(II). Biochem Biophys Res Commun 1996;229:648-52
98. Tamamura H, Xu Y, Hattori T, et al. A low-molecular-weight inhibitor against the chemokine receptor CXCR4: a strong anti-HIV peptide T140 Biochem Biophys Res Commun 1998;253:877-82
99. 7]-polyphemusin II), which specifically blocks T cell-line-tropic HIV-1 infection. Bioorg Med Chem 1998;6:1033-41
100. Marshall GR, Nauk A, Reddy PA, et al. Combinatorial chemistry of metal-binding ligands. Adv Supramol Chem 2001;8:175-243
101. Ye Y, Liu M, Kao JL, Marshall GR. Peptide-bond modification for metal coordination: peptides containing two hydroxamate groups. Biopolymers 2003;71:489-515
102. Poreddy AR, Schall OF, Osiek TA, et al. Hydroxamate-based iron chelators: combinatorial syntheses of desferrioxamine B analogues and evaluation of binding affinities. J Comb Chem 2004;6:239-54
103. Ye Y, Liu M, Kao JL, Marshall GR. Novel trihydroxamate-containing peptides: design, synthesis, and metal coordination. Biopolymers 2006;84:472-89
104. Akiyama M, Iesaki K, Katoh A, Shimizu K. N-Hydroxy amides. 5. Synthesis and properties of N-Hydroxypeptides having leucine enkephalin sequences. J Chem Soc-Perkin Trans 1 1986;851-55
105. Kip2 in cyclin-dependent kinase 2 inhibition and growth suppression. J Biol Chem 1998;273:16544-50
106. Liu Q, Berry D, Nash P, et al. Structural basis for specific binding of the gads SH3 domain to an RxxK motif-containing SLP-76 peptide: a novel mode of peptide recognition. Mol Cell 2003;11:471-81
107. 10-helical to α-helical transition of an oligopeptide in various solvents. J Am Chem Soc 1993;115:11594-5
108. Che Y, Brooks BR, Marshall GR. Protein recognition motifs: design of peptidomimetics of helix surfaces. Biopolymers 2007;86:288-97
109. Orner BP, Ernst JT, Hamilton AD. Toward proteomimetics: terphenyl derivatives as structural and functional mimics of extended regions of an α-helix. J Am Chem Soc 2001;123:5382-3
110. Ernst JT, Kutzki O, Debnath AK, et al. Design of a protein surface antagonist based on α-helix mimicry: inhibition of gp41 assembly and viral fusion. Angew Chem-Int Edit 2002;41:278-81
111. L antagonist based on α-helix mimicry. J Am Chem Soc 2002;124:11838-9
112. L. J Am Chem Soc 2005;127:10191-6
113. Yin H, Lee GI, Park HS, et al. Terphenyl-based helical mimetics that disrupt the p53/HDM2 interaction. Angew Chem-Int Edit 2005;44:2704-7
114. Jacoby E. Biphenyls as potential mimetics of protein α-helix. Bioorg Med Chem Lett 2002;12:891-3
115. L/Bak interaction. J Am Chem Soc 2005;127:5463-8
116. Davis JM, Truong A, Hamilton AD. α-helix mimetics designed to disrupt protein-protein interactions. Washington, DC: 230th ACS National Meeting, 2005
117. Rodriguez JM, Lee GI, Dhar D, Hamilton AD. Novel, simplified α-helix mimetics targeted to Bcl-xL. Chicago, IL: 233rd ACS National Meeting, 2007
118. Biros SM, Moisan L, Mann E, et al. Heterocyclic α-helix mimetics for targeting protein-protein interactions. Bioorg Med Chem Lett 2007;17:4641-5
119. L complex. Angew Chem-Int Edit 2003;42:535-9
120. Marshall GR, Bosshard HE. Angiotensin-II - studies on biologically-active conformation. Circ Res 1972;31:143-50
121. Marshall GR, Hodgkin EE, Langs DA, et al. Factors governing helical preference of peptides containing multiple α,α-dialkyl amino-acids. Proc Natl Acad Sci USA 1990;87:487-91
122. Garcia-Echeverria C, Chene P, Blommers MJJ, Furet P. Discovery of potent antagonists of the interaction between human double minute 2 and tumor suppressor p53. J Med Chem 2000;43:3205-8
123. Marqusee S, Baldwin RL. Helix stabilization By Glu- ... Lys+ salt bridges in short peptides of de novo design. Proc Natl Acad Sci USA 1987;84:8898-902
124. Albert JS, Hamilton AD. Stabilization of helical domains in short peptides using hydrophobic interactions. Biochemistry 1995;34:984-90
125. Butterfield SM, Patel PR, Waters ML. Contribution of aromatic interactions to α-helix stability. J Am Chem Soc 2002; 124:9751-5
126. FernandezRecio J, Vazquez A, Civera C, et al. The tryptophan/histidine interaction in α-helices. J Mol Biol 1997;267:184-97
127. Viguera AR, Serrano L. Side-chain interactions between sulfur-containing amino-acids and phenylalanine in α-helices. Biochemistry 1995; 34:8771-9
128. Jackson DY, King DS, Chmielewski J, et al. General-approach to the synthesis of short α-helical peptides. J Am Chem Soc 1991; 113:9391-2
129. Leduc AM, Trent JO, Wittliff JL, et al. Helix-stabilized cyclic peptides as selective inhibitors of steroid receptor-coactivator interactions. Proc Natl Acad Sci USA 2003;100:11273-8
130. Felix AM, Heimer EP, Wang CT, et al. Synthesis, biological-activity and conformational-analysis of cyclic GRF analogs. Int J Pept Protein Res 1988;32:441-54
131. Osapay G, Taylor JW. Multicyclic polypeptide model compounds. 2. Synthesis and conformational properties of a highly α-helical uncosapeptide constrained by 3 side-chain to side-chain lactam bridges. J Am Chem Soc 1992;114:6966-73
132. Shepherd NE, Hoang HN, Abbenante G, Fairlie DP. Single turn peptide alpha helices with exceptional stability in water. J Am Chem Soc 2005;127:2974-83
133. Blackwell HE, Grubbs RH. Highly efficient synthesis of covalently cross-linked peptide helices by ring-closing metathesis. Angew Chem-Int Edit 1998;37:3281-4
134. 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;122:5891-2
135. Phelan JC, Skelton NJ, Braisted AC, McDowell RS. A general method for constraining short peptides to an α-helical conformation. J Am Chem Soc 1997;119:455-60
136. Fujimoto K, Oimoto N, Katsuno K, Inouye M. Effective stabilisation of α-helical structures in short peptides with acetylenic cross-linking agents. Chem Commun 2004;1280-1
137. Ghadiri MR, Choi C. Secondary structure nucleation in peptides - transition-metal ion stabilized alpha-helices. J Am Chem Soc 1990;112:1630-2
138. Kelso MJ, Hoang HN, Appleton TG, Fairlie DP. The first solution stucture of a single α-helical turn. A pentapeptide α-helix stabilized by a metal clip. J Am Chem Soc 2000;122:10488-9
139. Ruan FQ, Chin YQ, Hopkins PB. Metal-ion enhanced helicity in synthetic peptides containing unnatural, metal-ligating residues. J Am Chem Soc 1990;112:9403-4
140. Gilbertson SR, Wang XF. Synthesis of (dicyclohexylphosphino)serine, its incorporation into a dodecapeptide, and the coordination of rhodium. J Org Chem 1996;61:434-5
141. Walensky LD, Kung AL, Escher I, et al. Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix. Science 2004;305:1466-70
142. Cabezas E, Satterthwait AC. The hydrogen bond mimic approach: solid-phase synthesis of a peptide stabilized as an α-helix with a hydrazone link. J Am Chem Soc 1999;121:3862-75
143. Chapman RN, Dimartino G, Arora PS. A highly stable short α-helix constrained by a main-chain hydrogen-bond surrogate. J Am Chem Soc 2004;126:12252-3
144. Calvo JC, Choconta KC, Diaz D, et al. An α-helix conformationally restricted peptide is recognized by cervical carcinoma patients' sera. J Med Chem 2003;46:5389-94
145. Kemp DS, Boyd JG, Muendel CC. The helical S-constant for alanine in water derived from template-nucleated helices. Nature 1991;352:451-4
146. Austin RE, Maplestone RA, Sefler AM, et al. Template for stabilization of a peptide α-helix: synthesis and evaluation of conformational effects by circular dichroism and NMR. J Am Chem Soc 1997;119:6461-72
147. Goodman CM, Choi S, Shandler S, DeGrado WF. Foldamers as versatile frameworks for the design and evolution of function. Nat Chem Biol 2007;3:252-62
148. Simon RJ, Kania RS, Zuckermann RN, et al. Peptoids - a modular approach to drug discovery. Proc Natl Acad Sci USA 1992;89:9367-71
149. Hara T, Durell SR, Myers MC, Appella DH. Probing the structural requirements of peptoids that inhibit HDM2-p53 interactions. J Am Chem Soc 2006;128:1995-2004
150. Gellman SH. Foldamers: a manifesto. Accounts Chem Res 1998;31:173-80
151. Seebach D, Kimmerlin T, Sebesta R, et al. How we drifted into peptide chemistry and where we have arrived at. Tetrahedron 2004;60:7455-506
152. 3-peptide 14-helix stability in water. J Am Chem Soc 2003;125:4022-3
153. Kritzer JA, Lear JD, Hodsdon ME, Schepartz A. Helical β-peptide inhibitors of the p53-hDM2 interaction. J Am Chem Soc 2004;126:9468-9
154. Stephens OM, Kim S, Welch BD, et al. Inhibiting HIV fusion with a β-peptide foldamer. J Am Chem Soc 2005;127:13126-7
155. Seebach D, Hook DF, Glattli A. Helices and other secondary structures of β- and γ-peptides. Biopolymers 2006;84:23-37
156. Baldauf C, Gunther R, Hofmann HJ. Helices in peptoids of α- and β-peptides. Phys Biol 2006;3:S1-S9
157. Baldauf C, Gunther R, Hofmann HJ. Helix formation in α,γ- and β,γ-hybrid peptides: theoretical insights into mimicry of α- and β-peptides. J Org Chem 2006;71:1200-8
158. Baldauf C, Gunther R, Hofmann HJ. Theoretical prediction of the basic helix types in α,β-hybrid peptides. Biopolymers 2006;84:408-13