Peptides containing β-amino acid patterns: Challenges and successes in medicinal chemistry

Journal of Medicinal Chemistry

Volumn 57, Issue 23, 2014, Pages 9718-9739

  Cabrele, Chiara ^a   Martinek, Tamás A ^b   Reiser, Oliver ^c   Berlicki, Łukasz ^d  

^a UNIVERSITY OF SALZBURG   (Austria)

^b UNIVERSITY OF SZEGED   (Hungary)

^c UNIVERSITY OF REGENSBURG   (Germany)

^d WROCLAW UNIVERSITY OF TECHNOLOGY   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA BETA OLIGOMER; ANGIOGENESIS INHIBITOR; ANGIOTENSIN RECEPTOR; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; ANTIFUNGAL AGENT; BETA AMINO ACID; BETA AMINO ACID SUBSTITUTION; BOMBESIN RECEPTOR; CALCITONIN GENE RELATED PEPTIDE RECEPTOR; GAMMA SECRETASE; GLUCAGON LIKE PEPTIDE 1 RECEPTOR; GONADORELIN; GONADORELIN RECEPTOR; HUMAN IMMUNODEFICIENCY VIRUS FUSION PROTEIN GP41 INHIBITOR; HYBRID PROTEIN; INTEGRIN RECEPTOR; INTERLEUKIN 8; LECTIN; NEUROPEPTIDE Y RECEPTOR; NEUROTENSIN RECEPTOR; OLIGOMER; OPIATE RECEPTOR; P53AD PROTEIN INHIBITOR; PARATHYROID HORMONE RECEPTOR 1; PEPTIDE DERIVATIVE; PROTEIN BCL 2 PROTEIN INHIBITOR; PROTEIN INHIBITOR; PROTEIN MDM2 INHIBITOR; SOMATOSTATIN RECEPTOR; UNCLASSIFIED DRUG; VASCULOTROPIN RECEPTOR; AMINO ACID; GNRHR PROTEIN, HUMAN; LIGAND; PEPTIDE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANTIANGIOGENIC ACTIVITY; ANTIFUNGAL ACTIVITY; BINDING SITE; BIOLOGICAL FUNCTIONS; BOMBESIN RECEPTOR SUBTYPE 3; CELL MEMBRANE PERMEABILITY; CONFOCAL LASER MICROSCOPY; CONFORMATION; DRUG HALF LIFE; DRUG MECHANISM; ENZYMATIC DEGRADATION; HUMAN; MEDICINAL CHEMISTRY; MEMBRANE DAMAGE; MOLECULAR RECOGNITION; NONHUMAN; PHYSICAL CHEMISTRY; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; RECEPTOR BINDING; REVIEW; STEREOCHEMISTRY; THROMBOCYTE AGGREGATION; THROMBOCYTE AGGREGATION INHIBITION; CHEMISTRY; PROTEIN CONFORMATION; STEREOISOMERISM;

AMINO ACID SEQUENCE; AMINO ACIDS; HUMANS; LIGANDS; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, LHRH; RECEPTORS, VASCULAR ENDOTHELIAL GROWTH FACTOR; STEREOISOMERISM;

EID: 84918498601     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm5010896     Document Type: Review

References (231)

1. Kaspar, A. A.; Reichert, J. M. Future directions for peptide therapeutics development Drug Discovery Today 2013, 18, 807-817
2. Horne, W. S. Peptide and peptoid foldamers in medicinal chemistry Expert Opin. Drug Discovery 2011, 6, 1247-1262
3. Koyack, M. J.; Cheng, R. P. Design and synthesis of beta-peptides with biological activity Methods Mol. Biol. 2006, 340, 95-109
4. Goodman, C. M.; Choi, S.; Shandler, S.; DeGrado, W. F. Foldamers as versatile frameworks for the design and evolution of function Nat. Chem. Biol. 2007, 3, 252-262
5. Cheng, R. P.; Gellman, S. H.; DeGrado, W. F. β-Peptides: from structure to function Chem. Rev. 2001, 101, 3219-3232
6. Seebach, D.; Beck, A. K.; Bierbaum, D. J. The world of beta- and gamma-peptides comprised of homologated proteinogenic amino acids and other components Chem. Biodiversity 2004, 1, 1111-1239
7. Gellman, S. H. Foldamers: a manifesto Acc. Chem. Res. 1998, 31, 173-180
8. Fülöp, F.; Martinek, T. A.; Tóth, G. K. Application of alicyclic beta-amino acids in peptide chemistry Chem. Soc. Rev. 2006, 35, 323-334
9. Horne, W. S.; Gellman, S. H. Foldamers with heterogeneous backbones Acc. Chem. Res. 2008, 41, 1399-1408
10. Martinek, T. A.; Fülöp, F. Peptidic foldamers: ramping up diversity Chem. Soc. Rev. 2012, 41, 687-702
11. Seebach, D.; Matthews, J. L. β-Peptides: a surprise at every turn Chem. Commun. 1997, 2015-2022
12. Pilsl, L. K.; Reiser, O. α/β-Peptide foldamers: state of the art Amino Acids 2011, 41, 709-718
13. Mándity, I. M.; Wéber, E.; Martinek, T. A.; Olajos, G.; Tóth, G. K.; Vass, E.; Fülöp, F. Design of peptidic foldamer helices: a stereochemical patterning approach Angew. Chem., Int. Ed. 2009, 48, 2171-2175
14. Berlicki, Ł.; Pilsl, L.; Wéber, E.; Mándity, I. M.; Cabrele, C.; Martinek, T. A.; Fülöp, F.; Reiser, O. Unique α,β- and α,α,β,β-peptide foldamers based on cis -β-aminocyclopentanecarboxylic acid Angew. Chem., Int. Ed. 2012, 51, 2208-2212
15. L recognition by a BH3-mimetic α/β-peptide generated by sequence-based design ChemBioChem 2011, 12, 2025-2032
16. Schmitt, M. A.; Weisblum, B.; Gellman, S. H. Interplay among folding, sequence, and lipophilicity in the antibacterial and hemolytic activities of alpha/beta-peptides J. Am. Chem. Soc. 2007, 129, 417-428
17. Hook, D. F.; Bindschädler, P.; Mahajan, Y. R.; Sebesta, R.; Kast, P.; Seebach, D. The proteolytic stability of designed beta-peptides containing alpha-peptide-bond mimics and of mixed alpha,beta-peptides: application to the construction of MHC-binding peptides Chem. Biodiversity 2005, 2, 591-632
18. Tew, G. N.; Scott, R. W.; Klein, M. L.; Degrado, W. F. De novo design of antimicrobial polymers, foldamers, and small molecules: from discovery to practical applications Acc. Chem. Res. 2010, 43, 30-39
19. Arvidsson, P. I.; Ryder, N. S.; Weiss, H. M.; Hook, D. F.; Escalante, J.; Seebach, D. Exploring the antibacterial and hemolytic activity of shorter- and longer-chain beta-, alpha,beta-, and gamma-peptides, and of beta-peptides from beta2-3-aza- and beta3-2-methylidene-amino acids bearing proteinogenic side chains-a survey Chem. Biodiversity 2005, 2, 401-420
20. Zasloff, M. Antimicrobial peptides of multicellular organisms Nature 2002, 415, 389-395
21. Zasloff, M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor Proc. Natl. Acad. Sci. U.S.A. 1987, 84, 5449-5453
22. Argiolas, A.; Pisano, J. J. Bombolitins, a new class of mast cell degranulating peptides from the venom of the bumblebee Megabombus pennsylvanicus J. Biol. Chem. 1985, 260, 1437-1444
23. Morishima, I.; Suginaka, S.; Ueno, T.; Hirano, H. Isolation and structure of cecropins, inducible antibacterial peptides, from the silkworm, Bombyx mori Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol. 1990, 95, 551-554
24. Hirai, Y.; Yasuhara, T.; Yoshida, H.; Nakajima, T.; Fujino, M.; Kitada, C. A new mast cell degranulating peptide "mastoparan" in the venom of Vespula lewisii Chem. Pharm. Bull. 1979, 27, 1942-1944
25. Méndez-Samperio, P. Recent advances in the field of antimicrobial peptides in inflammatory diseases Adv. Biomed. Res. 2013, 2, 50-50
26. Hamuro, Y.; Schneider, J. P.; DeGrado, W. F. De novo design of antibacterial β-peptides J. Am. Chem. Soc. 1999, 121, 12200-12201
27. Liu, D.; DeGrado, W. F. De novo design, synthesis, and characterization of antimicrobial β-peptides J. Am. Chem. Soc. 2001, 123, 7553-7559
28. Arvidsson, P. I.; Frackenpohl, J.; Ryder, N. S.; Liechty, B.; Petersen, F.; Zimmermann, H.; Camenisch, G. P.; Woessner, R.; Seebach, D. On the antimicrobial and hemolytic activities of amphiphilic beta-peptides ChemBioChem. 2001, 2, 771-773
29. Porter, E. A.; Wang, X.; Lee, H. S.; Weisblum, B.; Gellman, S. H. Non-haemolytic beta-amino-acid oligomers Nature 2000, 404, 565-565
30. Arvidsson, P. I.; Ryder, N. S.; Weiss, H. M.; Gross, G.; Kretz, O.; Woessner, R.; Seebach, D. Antibiotic and hemolytic activity of a beta2/beta3 peptide capable of folding into a 12/10-helical secondary structure ChemBioChem 2003, 4, 1345-1347
31. Raguse, T. L.; Porter, E. A.; Weisblum, B.; Gellman, S. H. Structure-activity studies of 14-helical antimicrobial β-peptides: probing the relationship between conformational stability and antimicrobial potency J. Am. Chem. Soc. 2002, 124, 12774-12785
32. Porter, E. A.; Weisblum, B.; Gellman, S. H. Use of parallel synthesis to probe structure-activity relationships among 12-helical β-peptides: evidence of a limit on antimicrobial activity J. Am. Chem. Soc. 2005, 127, 11516-11529
33. Schmitt, M. A.; Weisblum, B.; Gellman, S. H. Unexpected relationships between structure and function in α,β-peptides: antimicrobial foldamers with heterogeneous backbones J. Am. Chem. Soc. 2004, 126, 6848-6849
34. Rueping, M.; Mahajan, Y.; Sauer, M.; Seebach, D. Cellular uptake studies with beta-peptides ChemBioChem 2002, 3, 257-259
35. Umezawa, N.; Gelman, M. A.; Haigis, M. C.; Raines, R. T.; Gellman, S. H. Translocation of a beta-peptide across cell membranes J. Am. Chem. Soc. 2002, 124, 368-369
36. Kolesinska, B.; Podwysocka, D. J.; Rueping, M. A.; Seebach, D.; Kamena, F.; Walde, P.; Sauer, M.; Windschiegl, B.; Meyer-ács, M.; Vor der Brüggen, M.; Giehring, S. Permeation through phospholipid bilayers, skin-cell penetration, plasma stability, and CD spectra of α- and β-oligoproline derivatives Chem. Biodiversity 2013, 10, 1-38
37. Geueke, B.; Namoto, K.; Agarkova, I.; Perriard, J. C.; Kohler, H. P.; Seebach, D. Bacterial cell penetration by beta3-oligohomoarginines: indications for passive transfer through the lipid bilayer ChemBioChem 2005, 6, 982-985
38. Seebach, D.; Namoto, K.; Mahajan, Y. R.; Bindschädler, P.; Sustmann, R.; Kirsch, M.; Ryder, N. S.; Weiss, M.; Sauer, M.; Roth, C.; Werner, S.; Beer, H. D.; Munding, C.; Walde, P.; Voser, M. Chemical and biological investigations of beta-oligoarginines Chem. Biodiversity 2004, 1, 65-97
39. Hitz, T.; Iten, R.; Gardiner, J.; Namoto, K.; Walde, P.; Seebach, D. Interaction of alpha- and beta-oligoarginine-acids and amides with anionic lipid vesicles: a mechanistic and thermodynamic study Biochemistry 2006, 45, 5817-5829
40. Potocky, T. B.; Menon, A. K.; Gellman, S. H. Cytoplasmic and nuclear delivery of a TAT-derived peptide and a beta-peptide after endocytic uptake into HeLa cells J. Biol. Chem. 2003, 278, 50188-50194
41. Potocky, T. B.; Menon, A. K.; Gellman, S. H. Effects of conformational stability and geometry of guanidinium display on cell entry by beta-peptides J. Am. Chem. Soc. 2005, 127, 3686-3687
42. Potocky, T. B.; Silvius, J.; Menon, A. K.; Gellman, S. H. HeLa cell entry by guanidinium-rich beta-peptides: importance of specific cation-cell surface interactions ChemBioChem 2007, 8, 917-926
43. Kamena, F.; Monnanda, B.; Makou, D.; Capone, S.; Patora-Komisarska, K.; Seebach, D. On the mechanism of eukaryotic cell penetration by α- and β-oligoarginines-targeting infected erythrocytes Chem. Biodiversity 2011, 8, 1-12
44. Sparr, C.; Purkayastha, N.; Kolesinska, B.; Gengenbacher, M.; Amulic, B.; Matuschewski, K.; Seebach, D.; Kamena, F. Improved efficacy of fosmidomycin against Plasmodium and Mycobacterium species by combination with the cell-penetrating peptide octaarginine Antimicrob. Agents Chemother. 2013, 57, 4689-4698
45. Karlsson, A. J.; Pomerantz, W. C.; Weisblum, B.; Gellman, S. H.; Palecek, S. P. Antifungal activity from 14-helical beta-peptides J. Am. Chem. Soc. 2006, 128, 12630-12631
46. Lee, M.-R.; Raman, N.; Gellman, S. H.; Lynn, D. M.; Palecek, S. P. Hydrophobicity and helicity regulate antifungal activity of 14-helical β-peptides ACS Chem. Biol. 2014, 1613-1621
47. Karlsson, A. J.; Pomerantz, W. C.; Neilsen, K. J.; Gellman, S. H.; Palecek, S. P. Effect of sequence and structural properties on 14-helical β-peptide activity against Candida albicans planktonic cells and biofilms ACS Chem. Biol. 2009, 4, 567-579
48. Karlsson, A. J.; Flessner, R. M.; Gellman, S. H.; Lynn, D. M.; Palecek, S. P. Polyelectrolyte multilayers fabricated from antifungal β-peptides: design of surfaces that exhibit antifungal activity against Candida albicans Biomacromolecules 2010, 11, 2321-2328
49. Bultmann, H.; Brandt, C. R. Peptides containing membrane-transiting motifs inhibit virus entry J. Biol. Chem. 2002, 277, 36018-36023
50. Akkarawongsa, R.; Potocky, T. B.; English, E. P.; Gellman, S. H.; Brandt, C. R. Inhibition of herpes simplex virus type 1 infection by cationic beta-peptides Antimicrob. Agents Chemother. 2008, 52, 2120-2129
51. Keskin, O.; Gursoy, A.; Ma, B.; Nussinov, R. Principles of protein-protein interactions: what are the preferred ways for proteins to interact? Chem. Rev. 2008, 108, 1225-1244
52. Johnson, L. M.; Gellman, S. H. α-Helix mimicry with α/β-peptides Methods Enzymol. 2013, 523, 407-429
53. Wilson, A. J. Inhibition of protein-protein interactions using designed molecules Chem. Soc. Rev. 2009, 38, 3289-3300
54. Seebach, D.; Overhand, M.; Kuhnle, F. N. M.; Martinoni, B.; Oberer, L.; Hommel, U.; Widmer, H. Beta-peptides: synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a beta-hexapeptide in solution and its stability towards pepsin Helv. Chim. Acta 1996, 79, 913-941
55. Johnson, L. M.; Mortenson, D. E.; Yun, H. G.; Horne, W. S.; Ketas, T. J.; Lu, M.; Moore, J. P.; Gellman, S. H. Enhancement of α-helix mimicry by an α/β-peptide foldamer via incorporation of a dense ionic side-chain array J. Am. Chem. Soc. 2012, 134, 7317-7320
56. Bullock, B. N.; Jochim, A. L.; Arora, P. S. Assessing helical protein interfaces for inhibitor design J. Am. Chem. Soc. 2011, 133, 14220-14223
57. Jochim, A. L.; Arora, P. S. Systematic analysis of helical protein interfaces reveals targets for synthetic inhibitors ACS Chem. Biol. 2010, 5, 919-923
58. Watkins, A. M.; Arora, P. S. Anatomy of β-strands at protein-protein interfaces ACS Chem. Biol. 2014, 9, 1747-1754
59. Kussie, P. H.; Gorina, S.; Marechal, V.; Elenbaas, B.; Moreau, J.; Levine, A. J.; Pavletich, N. P. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain Science 1996, 274, 948-953
60. Chène, P. Inhibiting the p53-MDM2 interaction: an important target for cancer therapy Nat. Rev. Cancer 2003, 3, 102-109
61. Schon, O.; Friedler, A.; Bycroft, M.; Freund, S. M.; Fersht, A. R. Molecular mechanism of the interaction between MDM2 and p53 J. Mol. Biol. 2002, 323, 491-501
62. Böttger, A.; Böttger, V.; Garcia-Echeverria, C.; Chène, P.; Hochkeppel, H. K.; Sampson, W.; Ang, K.; Howard, S. F.; Picksley, S. M.; Lane, D. P. Molecular characterization of the hdm2-p53 interaction J. Mol. Biol. 1997, 269, 744-756
63. Massova, I.; Kollman, P. A. Computational alanine scanning to probe protein-protein interactions: a novel approach to evaluate binding free energies J. Am. Chem. Soc. 1999, 121, 8133-8143
64. Kritzer, J. A.; Lear, J. D.; Hodsdon, M. E.; Schepartz, A. Helical β-peptide inhibitors of the p53-hDM2 interaction J. Am. Chem. Soc. 2004, 126, 9468-9469
65. Kritzer, J. A.; Luedtke, N. W.; Harker, E. A.; Schepartz, A. A rapid library screen for tailoring beta-peptide structure and function J. Am. Chem. Soc. 2005, 127, 14584-14585
66. Bautista, A. D.; Appelbaum, J. S.; Craig, C. J.; Michel, J.; Schepartz, A. Bridged β3-peptide inhibitors of p53-hDM2 complexation: correlation between affinity and cell permeability J. Am. Chem. Soc. 2010, 132, 2904-2906
67. Harker, E. A.; Schepartz, A. Cell-permeable beta-peptide inhibitors of p53/hDM2 complexation ChemBioChem 2009, 10, 990-993
68. Michel, J.; Harker, E. A.; Tirado-Rives, J.; Jorgensen, W. L.; Schepartz, A. In silico improvement of beta3-peptide inhibitors of p53 x hDM2 and p53 x hDMX J. Am. Chem. Soc. 2009, 131, 6356-6357
69. Hintersteiner, M.; Kimmerlin, T.; Garavel, G.; Schindler, T.; Bauer, R.; Meisner, N. C.; Seifert, J. M.; Uhl, V.; Auer, M. A highly potent and cellularly active beta-peptidic inhibitor of the p53/hDM2 interaction ChemBioChem 2009, 10, 994-998
70. Patel, S.; Player, M. R. Small-molecule inhibitors of the p53-HDM2 interaction for the treatment of cancer Expert Opin. Invest. Drugs 2008, 17, 1865-1882
71. L proteins by synthetic Bcl-2 homology 3 domain peptide enhances the efficacy of chemotherapy J. Pharmacol. Exp. Ther. 2006, 316, 992-998
72. L-Bak peptide complex: recognition between regulators of apoptosis Science 1997, 275, 983-986
73. L: critical role of the molecular scaffold in protein surface recognition J. Am. Chem. Soc. 2005, 127, 11966-11968
74. L recognition: toward general strategies for foldamer-based inhibition of protein-protein interactions J. Am. Chem. Soc. 2007, 129, 139-154
75. L Angew. Chem., Int. Ed. 2009, 48, 4318-4322
76. L ChemBioChem 2007, 8, 903-916
77. Horne, W. S.; Boersma, M. D.; Windsor, M. A.; Gellman, S. H. Sequence-based design of α/β-peptide foldamers that mimic BH3 domains Angew. Chem., Int. Ed. 2008, 47, 2853-2856
78. Boersma, M. D.; Haase, H. S.; Peterson-Kaufman, K. J.; Lee, E. F.; Clarke, O. B.; Colman, P. M.; Smith, B. J.; Horne, W. S.; Fairlie, W. D.; Gellman, S. H. Evaluation of diverse α/β-backbone patterns for functional α-helix mimicry: analogues of the Bim BH3 domain J. Am. Chem. Soc. 2012, 134, 315-323
79. Bennett, J. S. Structure and function of the platelet integrin alphaIIbbeta3 J. Clin. Invest. 2005, 115, 3363-3369
80. Yin, H.; Slusky, J. S.; Berger, B. W.; Walters, R. S.; Vilaire, G.; Litvinov, R. I.; Lear, J. D.; Caputo, G. A.; Bennett, J. S.; DeGrado, W. F. Computational design of peptides that target transmembrane helices Science 2007, 315, 1817-1822
81. Shandler, S. J.; Korendovych, I. V.; Moore, D. T.; Smith-Dupont, K. B.; Streu, C. N.; Litvinov, R. I.; Billings, P. C.; Gai, F.; Bennett, J. S.; DeGrado, W. F. Computational design of a β-peptide that targets transmembrane helices J. Am. Chem. Soc. 2011, 133, 12378-12381
82. De Strooper, B.; Vassar, R.; Golde, T. The secretases: enzymes with therapeutic potential in Alzheimer disease Nat. Rev. Neurol. 2010, 6, 99-107
83. Das, C.; Berezovska, O.; Diehl, T. S.; Genet, C.; Buldyrev, I.; Tsai, J. Y.; Hyman, B. T.; Wolfe, M. S. Designed helical peptides inhibit an intramembrane protease J. Am. Chem. Soc. 2003, 125, 11794-11795
84. Kornilova, A. Y.; Bihel, F.; Das, C.; Wolfe, M. S. The initial substrate-binding site of gamma-secretase is located on presenilin near the active site Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 3230-3235
85. Imamura, Y.; Watanabe, N.; Umezawa, N.; Iwatsubo, T.; Kato, N.; Tomita, T.; Higuchi, T. Inhibition of gamma-secretase activity by helical beta-peptide foldamers J. Am. Chem. Soc. 2009, 131, 7353-7359
86. Imamura, Y.; Umezawa, N.; Osawa, S.; Shimada, N.; Higo, T.; Yokoshima, S.; Fukuyama, T.; Iwatsubo, T.; Kato, N.; Tomita, T.; Higuchi, T. Effect of helical conformation and side chain structure on γ-secretase inhibition by β-peptide foldamers: insight into substrate recognition J. Med. Chem. 2013, 56, 1443-1454
87. Harrison, S. C. Mechanism of membrane fusion by viral envelope proteins Adv. Virus Res. 2005, 64, 231-261
88. Weissenhorn, W.; Dessen, A.; Harrison, S. C.; Skehel, J. J.; Wiley, D. C. Atomic structure of the ectodomain from HIV-1 gp41 Nature 1997, 387, 426-430
89. Moore, J. P.; Doms, R. W. The entry of entry inhibitors: a fusion of science and medicine Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 10598-10602
90. Matthews, T.; Salgo, M.; Greenberg, M.; Chung, J.; DeMasi, R.; Bolognesi, D. Enfuvirtide: the first therapy to inhibit the entry of HIV-1 into host CD4 lymphocytes Nat. Rev. Drug Discovery 2004, 3, 215-225
91. Stephens, O. M.; Kim, S.; Welch, B. D.; Hodsdon, M. E.; Kay, M. S.; Schepartz, A. Inhibiting HIV fusion with a beta-peptide foldamer J. Am. Chem. Soc. 2005, 127, 13126-13127
92. Bautista, A. D.; Stephens, O. M.; Wang, L.; Domaoal, R. A.; Anderson, K. S.; Schepartz, A. Identification of a beta3-peptide HIV fusion inhibitor with improved potency in live cells Bioorg. Med. Chem. Lett. 2009, 19, 3736-3738
93. Horne, W. S.; Johnson, L. M.; Ketas, T. J.; Klasse, P. J.; Lu, M.; Moore, J. P.; Gellman, S. H. Structural and biological mimicry of protein surface recognition by alpha/beta-peptide foldamers Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 14751-14756
94. Frey, G.; Rits-Volloch, S.; Zhang, X. Q.; Schooley, R. T.; Chen, B.; Harrison, S. C. Small molecules that bind the inner core of gp41 and inhibit HIV envelope-mediated fusion Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 13938-13943
95. Johnson, L. M.; Horne, W. S.; Gellman, S. H. Broad distribution of energetically important contacts across an extended protein interface J. Am. Chem. Soc. 2011, 133, 10038-10041
96. Protein Design: Methods and Applications; Guerois, R.; López de la Paz, M., Eds.; Humana Press: Totowa, NJ, 2006; pp 1-299.
97. Gellman, S. H. Minimal model systems for beta sheet secondary structure in proteins Curr. Opin. Chem. Biol. 1998, 2, 717-725
98. Ramírez-Alvarado, M.; Kortemme, T.; Blanco, F. J.; Serrano, L. β-Hairpin and β-sheet formation in designed linear peptides Bioorg. Med. Chem. 1999, 7, 93-103
99. Mayo, K. H.; Ilyina, E.; Park, H. A recipe for designing water-soluble, beta-sheet-forming peptides Protein Sci. 1996, 5, 1301-1315
100. Searle, M. S. Insights into stabilizing weak interactions in designed peptide beta-hairpins Biopolymers 2004, 76, 185-195
101. Espinosa, J. F.; Syud, F. A.; Gellman, S. H. Analysis of the factors that stabilize a designed two-stranded antiparallel beta-sheet Protein Sci. 2002, 11, 1492-1505
102. Stanger, H. E.; Gellman, S. H. Rules for antiparallel β-sheet design: d -Pro-Gly is Superior to l -Asn-Gly for β-hairpin nucleation J. Am. Chem. Soc. 1998, 120, 4236-4237
103. Ramirez-Alvarado, M.; Blanco, F. J.; Serrano, L. De novo design and structural analysis of a model [beta]-hairpin peptide system Nat. Struct. Mol. Biol. 1996, 9, 604-612
104. de Alba, E.; Jiménez, M. A.; Rico, M.; Nieto, J. L. Conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solution Folding Des. 1996, 1, 133-144
105. Mayo, K. H.; Haseman, J.; Ilyina, E.; Gray, B. Designed beta-sheet-forming peptide 33mers with potent human bactericidal/permeability increasing protein-like bactericidal and endotoxin neutralizing activities Biochim. Biophys. Acta 1998, 1425, 81-92
106. Fernández-Escamilla, A. M.; Ventura, S.; Serrano, L.; Jiménez, M. A. Design and NMR conformational study of a beta-sheet peptide based on betanova and WW domains Protein Sci. 2006, 15, 2278-2289
107. Kortemme, T.; Ramírez-Alvarado, M.; Serrano, L. Design of a 20-amino acid, three-stranded beta-sheet protein Science 1998, 281, 253-256
108. Syud, F. A.; Stanger, H. E.; Mortell, H. S.; Espinosa, J. F.; Fisk, J. D.; Fry, C. G.; Gellman, S. H. Influence of strand number on antiparallel beta-sheet stability in designed three- and four-stranded beta-sheets J. Mol. Biol. 2003, 326, 553-568
109. de Alba, E.; Santoro, J.; Rico, M.; Jiménez, M. A. De novo design of a monomeric three-stranded antiparallel beta-sheet Protein Sci. 1999, 8, 854-865
110. Schenck, H. L.; Gellman, S. H. Use of a designed triple-stranded antiparallel β-sheet to probe β-sheet cooperativity in aqueous solution J. Am. Chem. Soc. 1998, 120, 4869-4870
111. Sharman, G. J.; Searle, M. S. Cooperative interaction between the three strands of a designed antiparallel β-sheet J. Am. Chem. Soc. 1998, 120, 5291-5300
112. Lim, A.; Makhov, A. M.; Saderholm, M. J.; Griffith, J. D.; Erickson, B. W. Biophysical characterization of betabellin 16D: a beta-sandwich protein that forms narrow fibrils which associate into broad ribbons Biochem. Biophys. Res. Commun. 1999, 264, 498-504
113. Lim, A.; Saderholm, M. J.; Makhov, A. M.; Kroll, M.; Yan, Y.; Perera, L.; Griffith, J. D.; Erickson, B. W. Engineering of betabellin-15D: a 64 residue beta sheet protein that forms long narrow multimeric fibrils Protein Sci. 1998, 7, 1545-1554
114. Yan, Y.; Erickson, B. W. Engineering of betabellin 14D: disulfide-induced folding of a beta-sheet protein Protein Sci. 1994, 3, 1069-1073
115. Robinson, J. A. Beta-hairpin peptidomimetics: design, structures and biological activities Acc. Chem. Res. 2008, 41, 1278-1288
116. Chung, Y. J.; Huck, B. R.; Christianson, L. A.; Stanger, H. E.; Krauthauser, S.; Powell, D. R.; Gellman, S. H. Stereochemical control of hairpin formation in beta-peptides containing dinipecotic acid reverse turn segments J. Am. Chem. Soc. 2000, 122, 3995-4004
117. Seebach, D.; Abele, S.; Gademann, K.; Jaun, B. Pleated sheets and turns of beta-peptides with proteinogenic side chains Angew. Chem., Int. Ed. 1999, 38, 1595-1597
118. Jones, C. R.; Qureshi, M. K.; Truscott, F. R.; Hsu, S. T.; Morrison, A. J.; Smith, M. D. A nonpeptidic reverse turn that promotes parallel sheet structure stabilized by C-H···O hydrogen bonds in a cyclopropane gamma-peptide Angew. Chem., Int. Ed. 2008, 47, 7099-7102
119. Qureshi, M. K.; Smith, M. D. Parallel sheet structure in cyclopropane gamma-peptides stabilized by C-H···O hydrogen bonds Chem. Commun. 2006, 5006-5008
120. Vass, E.; Strijowski, U.; Wollschläger, K.; Mándity, I. M.; Szilvágyi, G.; Jewgiński, M.; Gaus, K.; Royo, S.; Majer, Z.; Sewald, N.; Hollósi, M. VCD studies on cyclic peptides assembled from l -α-amino acids and a trans-2-aminocyclopentane- or trans-2-aminocyclohexane carboxylic acid J. Pept. Sci. 2010, 16, 613-620
121. Nowick, J. S. Exploring beta-sheet structure and interactions with chemical model systems Acc. Chem. Res. 2008, 41, 1319-1330
122. Cheng, P. N.; Liu, C.; Zhao, M.; Eisenberg, D.; Nowick, J. S. Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity Nat. Chem. 2012, 4, 927-933
123. Lengyel, G. A.; Frank, R. C.; Horne, W. S. Hairpin folding behavior of mixed α/β-peptides in aqueous solution J. Am. Chem. Soc. 2011, 133, 4246-4249
124. Lengyel, G. A.; Horne, W. S. Design strategies for the sequence-based mimicry of side-chain display in protein β-sheets by α/β-peptides J. Am. Chem. Soc. 2012, 134, 15906-15913
125. Reinert, Z. E.; Lengyel, G. A.; Horne, W. S. Protein-like tertiary folding behavior from heterogeneous backbones J. Am. Chem. Soc. 2013, 135, 12528-12531
126. Hegedüs, Z.; Wéber, E.; Kriston-Pál, é.; Makra, I.; Czibula, á.; Monostori, é.; Martinek, T. A. Foldameric α/β-peptide analogs of the β-sheet-forming antiangiogenic anginex: structure and bioactivity J. Am. Chem. Soc. 2013, 135, 16578-16584
127. Griffioen, A. W.; van der Schaft, D. W.; Barendsz-Janson, A. F.; Cox, A.; Struijker Boudier, H. A.; Hillen, H. F.; Mayo, K. H. Anginex, a designed peptide that inhibits angiogenesis Biochem. J. 2001, 354, 233-242
128. Dings, R. P.; van der Schaft, D. W.; Hargittai, B.; Haseman, J.; Griffioen, A. W.; Mayo, K. H. Anti-tumor activity of the novel angiogenesis inhibitor anginex Cancer Lett. 2003, 194, 55-66
129. van der Schaft, D. W.; Dings, R. P.; de Lussanet, Q. G.; van Eijk, L. I.; Nap, A. W.; Beets-Tan, R. G.; Bouma-Ter Steege, J. C.; Wagstaff, J.; Mayo, K. H.; Griffioen, A. W. The designer anti-angiogenic peptide anginex targets tumor endothelial cells and inhibits tumor growth in animal models FASEB J. 2002, 16, 1991-1993
130. Wang, J. B.; Wang, M. D.; Li, E. X.; Dong, D. F. Advances and prospects of anginex as a promising anti-angiogenesis and anti-tumor agent Peptides 2012, 38, 457-462
131. Thijssen, V. L.; Postel, R.; Brandwijk, R. J.; Dings, R. P.; Nesmelova, I.; Satijn, S.; Verhofstad, N.; Nakabeppu, Y.; Baum, L. G.; Bakkers, J.; Mayo, K. H.; Poirier, F.; Griffioen, A. W. Galectin-1 is essential in tumor angiogenesis and is a target for antiangiogenesis therapy Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 15975-15980
132. Mayo, K. H.; Ilyina, E. A folding pathway for betapep-4 peptide 33mer: from unfolded monomers and beta-sheet sandwich dimers to well-structured tetramers Protein Sci. 1998, 7, 358-368
133. Arroyo, M. M.; Mayo, K. H. NMR solution structure of the angiostatic peptide anginex Biochim. Biophys. Acta 2007, 1774, 645-651
134. Dings, R. P.; Arroyo, M. M.; Lockwood, N. A.; van Eijk, L. I.; Haseman, J. R.; Griffioen, A. W.; Mayo, K. H. Beta-sheet is the bioactive conformation of the anti-angiogenic anginex peptide Biochem. J. 2003, 373, 281-288
135. Ferrara, N.; Kerbel, R. S. Angiogenesis as a therapeutic target Nature 2005, 438, 967-974
136. Ferrara, N.; Hillan, K. J.; Gerber, H. P.; Novotny, W. Discovery and development of bevacizumab, an anti-VEGF antibody for treating cancer Nat. Rev. Drug Discovery 2004, 3, 391-400
137. Fairbrother, W. J.; Christinger, H. W.; Cochran, A. G.; Fuh, G.; Keenan, C. J.; Quan, C.; Shriver, S. K.; Tom, J. Y.; Wells, J. A.; Cunningham, B. C. Novel peptides selected to bind vascular endothelial growth factor target the receptor-binding site Biochemistry 1998, 37, 17754-17764
138. Haase, H. S.; Peterson-Kaufman, K. J.; Lan Levengood, S. K.; Checco, J. W.; Murphy, W. L.; Gellman, S. H. Extending foldamer design beyond α-helix mimicry: α/β-peptide inhibitors of vascular endothelial growth factor signaling J. Am. Chem. Soc. 2012, 134, 7652-7655
139. Webb, L. M.; Ehrengruber, M. U.; Clark-Lewis, I.; Baggiolini, M.; Rot, A. Binding to heparan sulfate or heparin enhances neutrophil responses to interleukin 8 Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 7158-7162
140. Zhang, Y. J.; Rutledge, B. J.; Rollins, B. J. Structure/activity analysis of human monocyte chemoattractant protein-1 (MCP-1) by mutagenesis. Identification of a mutated protein that inhibits MCP-1-mediated monocyte chemotaxis J. Biol. Chem. 1994, 269, 15918-15924
141. Hammond, M. E.; Shyamala, V.; Siani, M. A.; Gallegos, C. A.; Feucht, P. H.; Abbott, J.; Lapointe, G. R.; Moghadam, M.; Khoja, H.; Zakel, J.; Tekamp-Olson, P. Receptor recognition and specificity of interleukin-8 is determined by residues that cluster near a surface-accessible hydrophobic pocket J. Biol. Chem. 1996, 271, 8228-8235
142. David, R.; Günther, R.; Baumann, L.; Lühmann, T.; Seebach, D.; Hofmann, H. J.; Beck-Sickinger, A. G. Artificial chemokines: combining chemistry and molecular biology for the elucidation of interleukin-8 functionality J. Am. Chem. Soc. 2008, 130, 15311-15317
143. McLean, C. A.; Cherny, R. A.; Fraser, F. W.; Fuller, S. J.; Smith, M. J.; Beyreuther, K.; Bush, A. I.; Masters, C. L. Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimers disease Ann. Neurol. 1999, 46, 860-866
144. Näslund, J.; Haroutunian, V.; Mohs, R.; Davis, K. L.; Davies, P.; Greengard, P.; Buxbaum, J. D. Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline JAMA 2000, 12, 1571-1577
145. Walsh, D. M.; Klyubin, I.; Fadeeva, J. V.; Cullen, W. K.; Anwyl, R.; Wolfe, M. S.; Rowan, M. J.; Selkoe, D. J. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo Nature 2002, 416, 535-539
146. Cleary, J. P.; Walsh, D. M.; Hofmeister, J. J.; Shankar, G. M.; Kuskowski, M. A.; Selkoe, D. J.; Ashe, K. H. Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function Nat. Neurosci. 2005, 8, 79-84
147. Shankar, G. M.; Li, S.; Mehta, T. H.; Garcia-Munoz, A.; Shepardson, N. E.; Smith, I.; Brett, F. M.; Farrell, M. A.; Rowan, M. J.; Lemere, C. A.; Regan, C. M.; Walsh, D. M.; Sabatini, B. L.; Selkoe, D. J. Amyloid-beta protein dimers isolated directly from Alzheimers brains impair synaptic plasticity and memory Nat. Med. 2008, 14, 837-842
148. Walsh, D. M.; Selkoe, D. J. Deciphering the molecular basis of memory failure in Alzheimers disease Neuron 2004, 44, 181-193
149. Kamenetz, F.; Tomita, T.; Hsieh, H.; Seabrook, G.; Borchelt, D.; Iwatsubo, T.; Sisodia, S.; Malinow, R. APP processing and synaptic function Neuron 2003, 37, 925-937
150. Tjernberg, L. O.; Näslund, J.; Lindqvist, F.; Johansson, J.; Karlström, A. R.; Thyberg, J.; Terenius, L.; Nordstedt, C. Arrest of beta-amyloid fibril formation by a pentapeptide ligand J. Biol. Chem. 1996, 271, 8545-8548
151. Soto, C.; Kindy, M. S.; Baumann, M.; Frangione, B. Inhibition of Alzheimers amyloidosis by peptides that prevent beta-sheet conformation Biochem. Biophys. Res. Commun. 1996, 226, 672-680
152. Findeis, M. A.; Musso, G. M.; Arico-Muendel, C. C.; Benjamin, H. W.; Hundal, A. M.; Lee, J. J.; Chin, J.; Kelley, M.; Wakefield, J.; Hayward, N. J.; Molineaux, S. M. Modified-peptide inhibitors of amyloid beta-peptide polymerization Biochemistry 1999, 38, 6791-6800
153. Etienne, M. A.; Aucoin, J. P.; Fu, Y.; McCarley, R. L.; Hammer, R. P. Stoichiometric inhibition of amyloid beta-protein aggregation with peptides containing alternating alpha,alpha-disubstituted amino acids J. Am. Chem. Soc. 2006, 128, 3522-3523
154. Etienne, M. A.; Bett, C.; Aucoin, J. P.; Jensen, T. J.; McCarley, R. L.; Ajmo, T.; Herber, D.; Morgan, D.; Hammer, R. P. Stoichiometric inhibition of beta-amyloid fibrillogenesis using C(alpha,alpha)disubstituted amino acid containing peptides Am. Pept. Symp. 2006, 9, 471-472
155. Kokkoni, N.; Stott, K.; Amijee, H.; Mason, J. M.; Doig, A. J. N-Methylated peptide inhibitors of beta-amyloid aggregation and toxicity. Optimization of the inhibitor structure Biochemistry 2006, 45, 9906-9918
156. Bett, C. K.; Ngunjiri, J. N.; Serem, W. K.; Fontenot, K. R.; Hammer, R. P.; McCarley, R. L.; Garno, J. C. Structure-activity relationships in peptide modulators of β-amyloid protein aggregation: variation in α,α-disubstitution results in altered aggregate size and morphology ACS Chem. Neurosci. 2010, 1, 608-626
157. Chen, Z.; Krause, G.; Reif, B. Structure and orientation of peptide inhibitors bound to beta-amyloid fibrils J. Mol. Biol. 2005, 354, 760-776
158. Fülöp, L.; Mándity, I. M.; Juhász, G.; Szegedi, V.; Hetényi, A.; Wéber, E.; Bozsó, Z.; Simon, D.; Benko, M.; Király, Z.; Martinek, T. A. A foldamer-dendrimer conjugate neutralizes synaptotoxic β-amyloid oligomers PLoS One 2012, 7, e39485
159. Thorens, B. Expression cloning of the pancreatic beta cell receptor for the gluco-incretin hormone glucagon-like peptide 1 Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 8641-8645
160. Norgren, A. S.; Geitmann, M.; Danielson, U. H.; Arvidsson, P. I. Biomolecular recognition of glycosylated beta(3)-peptides, by GaINAc specific lectins J. Mol. Recognit. 2007, 20, 132-138
161. Kaszowska, M.; Norgren, A. S.; Arvidson, P. I.; Sandström, C. Studies on the interactions between glycosylated beta3-peptides and the lectin Vicia villosa by saturation transfer difference NMR spectroscopy Carbohydr. Res. 2009, 344, 2577-2580
162. Cabrele, C.; Beck-Sickinger, A. G. Molecular characterization of the ligand-receptor interaction of the neuropeptide Y family J. Pept. Sci. 2000, 6, 97-122
163. Yulyaningsih, E.; Zhang, L.; Herzog, H.; Sainsbury, A. NPY receptors as potential targets for anti-obesity drug development Br. J. Pharmacol. 2011, 163, 1170-1202
164. Bader, R.; Bettio, A.; Beck-Sickinger, A. G.; Zerbe, O. Structure and dynamics of micelle-bound neuropeptide Y: comparison with unligated NPY and implications for receptor selection J. Mol. Biol. 2001, 305, 307-329
165. Lerch, M.; Gafner, V.; Bader, R.; Christen, B.; Folkers, G.; Zerbe, O. Bovine pancreatic polypeptide (bPP) undergoes significant changes in conformation and dynamics upon binding to DPC micelles J. Mol. Biol. 2002, 322, 1117-1133
166. Koglin, N.; Zorn, C.; Beumer, R.; Cabrele, C.; Bubert, C.; Sewald, N.; Reiser, O.; Beck-Sickinger, A. G. Analogues of neuropeptide Y containing beta-aminocyclopropane carboxylic acids are the shortest linear peptides that are selective for the Y1 receptor Angew. Chem., Int. Ed. 2003, 42, 202-205
167. Berlicki, Ł.; Kaske, M.; Gutierrez-Abad, R.; Bernhardt, G.; Illa, O.; Ortuño, R. M.; Cabrele, C.; Buschauer, A.; Reiser, O. Replacement of Thr32 and Gln34 in the C-terminal neuropeptide Y fragment 25-36 by cis -cyclobutane- and cis -cyclopentane β-amino acids shifts selectivity toward the Y4 receptor J. Med. Chem. 2013, 56, 8422-8431
168. Mustain, W. C.; Rychahou, P. G.; Evers, B. M. The role of neurotensin in physiologic and pathologic processes Curr. Opin. Endocrinol., Diabetes Obes. 2011, 18, 75-82
169. Seebach, D.; Lukaszuk, A.; Patora-Komisarska, K.; Podwysocka, D.; Gardiner, J.; Ebert, M. O.; Reubi, J. C.; Cescato, R.; Waser, B.; Gmeiner, P.; Hübner, H.; Rougeot, C. On the terminal homologation of physiologically active peptides as a means of increasing stability in human serum-neurotensin, opiorphin, B27-KK10 epitope, NPY Chem. Biodiversity 2011, 8, 711-739
170. Sparr, C.; Purkayastha, N.; Yoshinari, T.; Seebach, D.; Maschauer, S.; Prante, O.; Hübner, H.; Gmeiner, P.; Kolesinska, B.; Cescato, R.; Waser, B.; Reubi, J. C. Syntheses, receptor bindings, in vitro and in vivo stabilities and biodistributions of DOTA-neurotensin(8-13) derivatives containing β-amino acid residues-a lesson about the importance of animal experiments Chem. Biodiversity 2013, 10, 2101-2121
171. Hoyer, D.; Bell, G. I.; Berelowitz, M.; Epelbaum, J.; Feniuk, W.; Humphrey, P. P.; OCarroll, A. M.; Patel, Y. C.; Schonbrunn, A.; Taylor, J. E. Classification and nomenclature of somatostatin receptors Trends Pharmacol. Sci. 1995, 16, 86-88
172. Hofland, L. J.; Visser-Wisselaar, H. A.; Lamberts, S. W. Somatostatin analogs: clinical application in relation to human somatostatin receptor subtypes Biochem. Pharmacol. 1995, 50, 287-297
173. Bauer, W.; Briner, U.; Doepfner, W.; Haller, R.; Huguenin, R.; Marbach, P.; Petcher, T. J.; Pless, J. SMS 201-995: a very potent and selective octapeptide analogue of somatostatin with prolonged action Life Sci. 1982, 31, 1133-1140
174. Gademann, K.; Kimmerlin, T.; Hoyer, D.; Seebach, D. Peptide folding induces high and selective affinity of a linear and small beta-peptide to the human somatostatin receptor 4 J. Med. Chem. 2001, 44, 2460-2468
175. Gademann, K.; Ernst, M.; Hoyer, D.; Seebach, D. Synthesis and biological evaluation of a cyclo-beta-tetrapeptide as a somatostatin analogue Angew. Chem., Int. Ed. 1999, 38, 1223-1226
176. Seebach, D.; Rueping, M.; Arvidsson, P. I.; Kimmerlin, T.; Micuch, P.; Noti, C.; Langenegger, D.; Hoyer, D. Linear, Peptidase-resistant beta2/beta3-di- and alpha/beta3-tetrapeptide derivatives with nanomolar affinities to a human somatostatin receptor, preliminary communication Helv. Chim. Acta 2001, 84, 3503-3510
177. Seebach, D.; Dubost, E.; Mathad, R. I.; Jaun, B.; Limbach, M.; Loweneck, M.; Flogel, O.; Gardiner, J.; Capone, S.; Beck, A. K.; Widmer, H.; Langenegger, D.; Monna, D.; Hoyer, D. New open-chain and cyclic tetrapeptides, consisting of α-, β2-, and β3-amino-acid residues, as somatostatin mimics-a survey Helv. Chim. Acta 2008, 91, 1736-1786
178. Kutscher, B.; Bernd, M.; Beckers, T.; Polymeropoulos, E. E.; Engel, J. Chemistry and molecular biology in the search for new LHRH antagonists Angew. Chem., Int. Ed. Engl. 1997, 36, 2148-2161
179. Schultze-Mosgau, A.; Griesinger, G.; Altgassen, C.; von Otte, S.; Hornung, D.; Diedrich, K. New developments in the use of peptide gonadotropin-releasing hormone antagonists versus agonists Expert. Opin. Invest. Drugs 2005, 14, 1085-1097
180. Monahan, M. W.; Amoss, M. S.; Anderson, H. A.; Vale, W. Synthetic analogs of the hypothalamic luteinizing hormone releasing factor with increased agonist or antagonist properties Biochemistry 1973, 12, 4616-4620
181. Langer, O.; Kählig, H.; Zierler-Gould, K.; Bats, J. W.; Mulzer, J. A bicyclic cispentacin derivative as a novel reverse turn inducer in a GnRH mimetic J. Org. Chem. 2002, 67, 6878-6883
182. Siryk-Bathgate, A.; Dabul, S.; Lymperopoulos, A. Current and future G protein-coupled receptor signaling targets for heart failure therapy Drug Des., Dev. Ther. 2013, 7, 1209-1222
183. Jones, E. S.; Del Borgo, M. P.; Kirsch, J. F.; Clayton, D.; Bosnyak, S.; Welungoda, I.; Hausler, N.; Unabia, S.; Perlmutter, P.; Thomas, W. G.; Aguilar, M. I.; Widdop, R. E. A single beta-amino acid substitution to angiotensin II confers AT2 receptor selectivity and vascular function Hypertension 2011, 57, 570-576
184. Tzakos, A. G.; Bonvin, A. M.; Troganis, A.; Cordopatis, P.; Amzel, M. L.; Gerothanassis, I. P.; van Nuland, N. A. On the molecular basis of the recognition of angiotensin II (AII). NMR structure of AII in solution compared with the X-ray structure of AII bound to the mAb Fab131 Eur. J. Biochem. 2003, 270, 849-860
185. Garcia, K. C.; Ronco, P. M.; Verroust, P. J.; Brünger, A. T.; Amzel, L. M. Three-dimensional structure of an angiotensin II-Fab complex at 3 Å: hormone recognition by an anti-idiotypic antibody Science 1992, 257, 502-507
186. Nikiforovich, G. V.; Kao, J. L.; Plucinska, K.; Zhang, W. J.; Marshall, G. R. Conformational analysis of two cyclic analogs of angiotensin: implications for the biologically active conformation Biochemistry 1994, 33, 3591-3598
187. Ohki-Hamazaki, H.; Watase, K.; Yamamoto, K.; Ogura, H.; Yamano, M.; Yamada, K.; Maeno, H.; Imaki, J.; Kikuyama, S.; Wada, E.; Wada, K. Mice lacking bombesin receptor subtype-3 develop metabolic defects and obesity Nature 1997, 390, 165-169
188. Mantey, S. A.; Coy, D. H.; Pradhan, T. K.; Igarashi, H.; Rizo, I. M.; Shen, L.; Hou, W.; Hocart, S. J.; Jensen, R. T. Rational design of a peptide agonist that interacts selectively with the orphan receptor, bombesin receptor subtype 3 J. Biol. Chem. 2001, 276, 9219-9229
189. Janecka, A.; Fichna, J.; Janecki, T. Opioid receptors and their ligands Curr. Top. Med. Chem. 2004, 4, 1-17
190. Waldhoer, M.; Bartlett, S. E.; Whistler, J. L. Opioid receptors Annu. Rev. Biochem. 2004, 73, 953-990
191. Lesma, G.; Salvadori, S.; Airaghi, F.; Murray, T. F.; Recca, T.; Sacchetti, A.; Balboni, G.; Silvani, A. Structural and biological exploration of Phe3-Phe4-modified endomorphin-2 peptidomimetics ACS Med. Chem. Lett. 2013, 4, 795-799
192. Zamfirova, R.; Pavlov, N.; Todorov, P.; Mateeva, P.; Martinez, J.; Calmès, M.; Naydenova, E. Synthesis and changes in affinity for NOP and opioid receptors of novel hexapeptides containing β(2)-tryptophan analogues Bioorg. Med. Chem. Lett. 2013, 23, 4052-4055
193. Liu, X.; Wang, Y.; Xing, Y.; Yu, J.; Ji, H.; Kai, M.; Wang, Z.; Wang, D.; Zhang, Y.; Zhao, D.; Wang, R. Design, synthesis, and pharmacological characterization of novel endomorphin-1 analogues as extremely potent μ-opioid agonists J. Med. Chem. 2013, 56, 3102-3114
194. Podwysocka, D.; Kosson, P.; Lipkowski, A. W.; Olma, A. TAPP analogs containing β3-homo-amino acids: synthesis and receptor binding J. Pept. Sci. 2012, 18, 556-559
195. Wang, Y.; Xing, Y.; Liu, X.; Ji, H.; Kai, M.; Chen, Z.; Yu, J.; Zhao, D.; Ren, H.; Wang, R. A new class of highly potent and selective endomorphin-1 analogues containing α-methylene-β-aminopropanoic acids (map) J. Med. Chem. 2012, 55, 6224-6236
196. Keresztes, A.; Birkás, E.; Páhi, A.; Tóth, G.; Bakota, L.; Gulya, K.; Szücs, M. Pharmacology of a new tritiated endomorphin-2 analog containing the proline mimetic cis -2-aminocyclohexanecarboxylic acid Peptides 2011, 32, 722-728
197. Mallareddy, J. R.; Borics, A.; Keresztes, A.; Kövér, K. E.; Tourwé, D.; Tóth, G. Design, synthesis, pharmacological evaluation, and structure-activity study of novel endomorphin analogues with multiple structural modifications J. Med. Chem. 2011, 54, 1462-1472
198. Giordano, C.; Sansone, A.; Masi, A.; Lucente, G.; Punzi, P.; Mollica, A.; Pinnen, F.; Feliciani, F.; Cacciatore, I.; Davis, P.; Lai, J.; Ma, S. W.; Porreca, F.; Hruby, V. Synthesis and activity of endomorphin-2 and morphiceptin analogues with proline surrogates in position 2 Eur. J. Med. Chem. 2010, 45, 4594-4600
199. Wilczyńska, D.; Kosson, P.; Kwasiborska, M.; Ejchart, A.; Olma, A. Synthesis and receptor binding of opioid peptide analogues containing beta3-homo-amino acids J. Pept. Sci. 2009, 15, 777-782
200. Keresztes, A.; Szucs, M.; Borics, A.; Kövér, K. E.; Forró, E.; Fülöp, F.; Tömböly, C.; Péter, A.; Páhi, A.; Fábián, G.; Murányi, M.; Tóth, G. New endomorphin analogues containing alicyclic beta-amino acids: influence on bioactive conformation and pharmacological profile J. Med. Chem. 2008, 51, 4270-4279
201. Toth, G.; Keresztes, A.; Toemboely, C.; Peter, A.; Fueloep, F.; Tourwe, D.; Navratilova, E.; Varga, E.; Roeske, W. R.; Yamamura, H. I.; Szuecs, M.; Borsodi, A. New endomorphin analogs with μ-agonist and δ-antagonist properties Pure Appl. Chem. 2004, 76, 951-957
202. Lesma, G.; Salvadori, S.; Airaghi, F.; Bojnik, E.; Borsodi, A.; Recca, T.; Sacchetti, A.; Balboni, G.; Silvani, A. Synthesis, pharmacological evaluation and conformational investigation of endomorphin-2 hybrid analogues Mol. Diversity 2013, 17, 19-31
203. Yamazaki, T.; Pröbsti, A.; Schiller, P. W.; Goodman, M. Biological and conformational studies of [Val4]morphiceptin and [ d -Val4]morphiceptin analogs incorporating cis -2-aminocyclopentane carboxylic acid as a peptidomimetic for proline Int. J. Pept. Protein Res. 1991, 37, 364-381
204. Mierke, D. F.; Nössner, G.; Schiller, P. W.; Goodman, M. Morphiceptin analogs containing 2-aminocyclopentane carboxylic acid as a peptidomimetic for proline Int. J. Pept. Protein Res. 1990, 35, 35-45
205. Cardillo, G.; Gentilucci, L.; Qasem, A. R.; Sgarzi, F.; Spampinato, S. Endomorphin-1 analogues containing beta-proline are mu-opioid receptor agonists and display enhanced enzymatic hydrolysis resistance J. Med. Chem. 2002, 45, 2571-2578
206. 2): a potent and specific agonist for morphine (mu) receptors Science 1981, 212, 75-77
207. Zadina, J. E.; Hackler, L.; Ge, L. J.; Kastin, A. J. A potent and selective endogenous agonist for the mu-opiate receptor Nature 1997, 386, 499-502
208. Dillon, J. S.; Tanizawa, Y.; Wheeler, M. B.; Leng, X. H.; Ligon, B. B.; Rabin, D. U.; Yoo-Warren, H.; Permutt, M. A.; Boyd, A. E. Cloning and functional expression of the human glucagon-like peptide-1 (GLP-1) receptor Endocrinology 1993, 133, 1907-1910
209. Drucker, D. J. The biology of incretin hormones Cell Metab. 2006, 3, 153-165
210. Lovshin, J. A.; Drucker, D. J. Incretin-based therapies for type 2 diabetes mellitus Nat. Rev. Endocrinol. 2009, 5, 262-269
211. Underwood, C. R.; Garibay, P.; Knudsen, L. B.; Hastrup, S.; Peters, G. H.; Rudolph, R.; Reedtz-Runge, S. Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor J. Biol. Chem. 2010, 285, 723-730
212. Inooka, H.; Ohtaki, T.; Kitahara, O.; Ikegami, T.; Endo, S.; Kitada, C.; Ogi, K.; Onda, H.; Fujino, M.; Shirakawa, M. Conformation of a peptide ligand bound to its G-protein coupled receptor Nat. Struct. Biol. 2001, 8, 161-165
213. Denton, E. V.; Craig, C. J.; Pongratz, R. L.; Appelbaum, J. S.; Doerner, A. E.; Narayanan, A.; Shulman, G. I.; Cline, G. W.; Schepartz, A. A β-peptide agonist of the GLP-1 receptor, a class B GPCR Org. Lett. 2013, 15, 5318-5321
214. Brain, S. D.; Grant, A. D. Vascular actions of calcitonin gene-related peptide and adrenomedullin Physiol. Rev. 2004, 84, 903-934
215. Edvinsson, L.; Sams, A.; Jansen-Olesen, I.; Tajti, J.; Kane, S. A.; Rutledge, R. Z.; Koblan, K. S.; Hill, R. G.; Longmore, J. Characterisation of the effects of a non-peptide CGRP receptor antagonist in SK-N-MC cells and isolated human cerebral arteries Eur. J. Pharmacol. 2001, 415, 39-44
216. Carpenter, K. A.; Schmidt, R.; von Mentzer, B.; Haglund, U.; Roberts, E.; Walpole, C. Turn structures in CGRP C-terminal analogues promote stable arrangements of key residue side chains Biochemistry 2001, 40, 8317-8325
217. Lang, M.; De Pol, S.; Baldauf, C.; Hofmann, H. J.; Reiser, O.; Beck-Sickinger, A. G. Identification of the key residue of calcitonin gene related peptide (CGRP) 27-37 to obtain antagonists with picomolar affinity at the CGRP receptor J. Med. Chem. 2006, 49, 616-624
218. Jüppner, H.; Abou-Samra, A. B.; Freeman, M.; Kong, X. F.; Schipani, E.; Richards, J.; Kolakowski, L. F.; Hock, J.; Potts, J. T.; Kronenberg, H. M. A G protein-linked receptor for parathyroid hormone and parathyroid hormone-related peptide Science 1991, 254, 1024-1026
219. Bukata, S. V.; Puzas, J. E. Orthopedic uses of teriparatide Curr. Osteoporos. Rep. 2010, 8, 28-33
220. Peggion, E.; Mammi, S.; Schievano, E.; Silvestri, L.; Schiebler, L.; Bisello, A.; Rosenblatt, M.; Chorev, M. Structure-function studies of analogues of parathyroid hormone (PTH)-1-34 containing beta-amino acid residues in positions 11-13 Biochemistry 2002, 41, 8162-8175
221. Coller, B. S. Platelets and thrombolytic therapy N. Engl. J. Med. 1990, 322, 33-42
222. Mousa, S. A.; Cheresh, D. A. Recent advances in cell adhesion molecules and extracellular matrix proteins: potential clinical implications Drug Discovery Today 1997, 2, 187-199
223. Scarborough, R. M. Structure-activity relationships of beta-amino acid-containing integrin antagonists Curr. Med. Chem. 1999, 6, 971-981
224. 1-integrin-mediated adhesion by dehydro-β-amino acids containing peptidomimetics Eur. J. Med. Chem. 2013, 66, 258-268
225. Hayashi, Y.; Katada, J.; Harada, T.; Tachiki, A.; Iijima, K.; Takiguchi, Y.; Muramatsu, M.; Miyazaki, H.; Asari, T.; Okazaki, T.; Sato, Y.; Yasuda, E.; Yano, M.; Uno, I.; Ojima, I. GPIIb/IIIa integrin antagonists with the new conformational restriction unit, trisubstituted beta-amino acid derivatives, and a substituted benzamidine structure J. Med. Chem. 1998, 41, 2345-2360
226. Hoekstra, W. J.; Maryanoff, B. E.; Damiano, B. P.; Andrade-Gordon, P.; Cohen, J. H.; Costanzo, M. J.; Haertlein, B. J.; Hecker, L. R.; Hulshizer, B. L.; Kauffman, J. A.; Keane, P.; McComsey, D. F.; Mitchell, J. A.; Scott, L.; Shah, R. D.; Yabut, S. C. Potent, orally active GPIIb/IIIa antagonists containing a nipecotic acid subunit. Structure-activity studies leading to the discovery of RWJ-53308 J. Med. Chem. 1999, 42, 5254-5265
227. Aumailley, M.; Gurrath, M.; Müller, G.; Calvete, J.; Timpl, R.; Kessler, H. Arg-Gly-Asp constrained within cyclic pentapeptides. Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1 FEBS Lett. 1991, 291, 50-54
228. Gurrath, M.; Müller, G.; Kessler, H.; Aumailley, M.; Timpl, R. Conformation/activity studies of rationally designed potent anti-adhesive RGD peptides Eur. J. Biochem. 1992, 210, 911-921
229. Urman, S.; Gaus, K.; Yang, Y.; Strijowski, U.; Sewald, N.; De Pol, S.; Reiser, O. The constrained amino acid beta-Acc confers potency and selectivity to integrin ligands Angew. Chem., Int. Ed. 2007, 46, 3976-3978
230. Karle, I. L.; Pramanik, A.; Banerjee, A.; Bhattacharjya, S.; Balaram, P. ω-Amino acids in peptide design. Crystal structures and solution conformations of peptide helices containing a β-alanyl-γ-aminobutyryl segment J. Am. Chem. Soc. 1999, 119, 9087-9095
231. Guo, L.; Almeida, A. M.; Zhang, W.; Reidenbach, A. G.; Choi, S. H.; Guzei, I. A.; Gellman, S. H. Helix formation in preorganized beta/gamma-peptide foldamers: hydrogen-bond analogy to the alpha-helix without alpha-amino acid residues J. Am. Chem. Soc. 2010, 132, 7868-7869