Helical structures of unnatural peptides for biological applications

Crisma M, Formaggio F, Moretto A, Toniolo C. Peptide helices based on α-amino acids. Biopolymers. 2006; 84(1):3–12. Guichard G, Huc I, Synthetic foldamers. Chem Commun. 2011; 47(21):5933–5941. Goodman CM, Choi S, Shandler S, DeGrado WF. Foldamers as versatile frameworks for the design and evolution of function. Nat Chem Biol. 2007; 3(5):252–262. Gellman SH. Foldamers: A manifesto. Acc Chem Res. 1998; 31(4):173–180. Cheng RP, Gellman SH, DeGrado WF. beta-peptides: From structure to function. Chem Rev. 2001; 101(10):3219–3232. Seebach D, Hook DF, Glättli A. Helices and other secondary structures of β- and γ-peptides. Peptide Sci. 2006; 84(1):23–37. Pilsl LKA, Reiser O. α/β-Peptide foldamers: State of the art. Amino Acids. 2011; 41(3):709–718. Martinek TA, Fulop F. Peptidic foldamers: Ramping up diversity. Chem Soc Rev. 2012; 41(2):687–702. Hill DJ, Mio MJ, Prince RB, Hughes TS, Moore JS. A field guide to foldamers. Chem Rev. 2001; 101(12):3893–4011. Appella DH, Christianson LA, Karle IL, Powell DR, Gellman SH. β-Peptide foldamers: Robust helix formation in a new family of β-Amino acid oligomers. J Am Chem Soc. 1996; 118(51):13071–13072. Seebach D, Overhand M, Kühnle FNM, Martinoni B, Oberer L, Hommel U, Widmer H. β-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 β-hexapeptide in solution and its stability towards pepsin. Helv Chim Acta. 1996; 79(4):913–941. Appella DH, Christianson LA, Klein DA, Powell DR, Huang X, Barchi JJ, Gellman SH. Residue-based control of helix shape in β-peptide oligomers. Nature. 1997; 387(6631):381–384. Porter EA, Wang X, Lee H-S, Weisblum B, Gellman SH. Antibiotics: Non-haemolytic β-amino acid oligomers. Nature. 2000; 404(6778):565. English EP, Chumanov RS, Gellman SH, Compton T. Rational development of β-peptide inhibitors of human cytomegalovirus entry. J Biol Chem. 2006; 281(5):2661–2667. Seebach D, Abele S, Gademann K, Guichard G, Hintermann T, Jaun B, Matthews JL, Schreiber JV, Oberer L, Hommel U, Widmer H. β2- and β3-peptides with proteinaceous side chains: Synthesis and solution structures of constitutional isomers, a novel helical secondary structure and the influence of solvation and hydrophobic interactions on folding. Helv Chim Acta. 1998; 81(5-8):932–982. Seebach D, Matthews JL. β-Peptides: A surprise at every turn. Chem Commun. 1997; (21):2015–2022. Lee M-R, Raguse TL, Schinnerl M, Pomerantz WC, Wang X, Wipf P, Gellman SH. Origins of the high 14-helix propensity of cyclohexyl-rigidified residues in β-peptides. Org Lett. 2007; 9(9):1801–1804. Podlech J, Seebach D, The Arndt-Eistert reaction in peptide chemistry: A facile access to homopeptides. Angew Chem Int Edit. 1995; 34(4):471–472. Hamuro Y, Schneider JP, DeGrado WF. De novo design of antibacterial β-peptides. J Am Chem Soc. 1999; 121(51):12200–12201. Epand RF, Raguse TL, Gellman SH, Epand RM. Antimicrobial 14-helical β-peptides: Potent bilayer disrupting agents?. Biochemistry. 2004; 43(29):9527–9535. Karlsson AJ, Pomerantz WC, Weisblum B, Gellman SH, Palecek SP. Antifungal activity from 14-helical β-peptides. J Am Chem Soc. 2006; 128(39):12630–12631. Daniels DS, Petersson EJ, Qiu JX, Schepartz A. High-resolution structure of a β-peptide bundle. J Am Chem Soc. 2007; 129(6):1532–1533. Park J-S, Lee H-S, Lai JR, Kim BM, Gellman SH. Accommodation of α-substituted residues in the β-peptide 12-helix: Expanding the range of substitution patterns available to a foldamer scaffold. J Am Chem Soc. 2003; 125(28):8539–8545. LePlae PR, Fisk JD, Porter EA, Weisblum B, Gellman SH. Tolerance of acyclic residues in the β-peptide 12-helix: Access to diverse side-chain arrays for biological applications. J Am Chem Soc. 2002; 124(24):6820–6821. Choi SH, Guzei IA, Spencer LC, Gellman SH. Crystallographic characterization of 12-helical secondary structure in β-peptides containing side chain groups. J Am Chem Soc. 2010; 132(39):13879–13885. Peelen TJ, Chi Y, English EP, Gellman SH. Synthesis of 4,4-disubstituted 2-aminocyclopentanecarboxylic acid derivatives and their incorporation into 12-helical β-peptides. Org Lett. 2004; 6(24):4411–4414. Horne WS, Gellman SH. Foldamers with heterogeneous backbones. Acc Chem Res. 2008; 41(10):1399–13408. 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 Edit. 2004; 43(4):505–510. De Pol S, Zorn C, Klein CD, Zerbe O, Reiser O. Surprisingly stable helical conformations in α/β-peptides by incorporation of cis-β-aminocyclopropane carboxylic acids. Angew Chem Int Edit. 2004; 43(4):511–514. Schmitt MA, Weisblum B, Gellman SH. Unexpected relationships between structure and function in α,β-peptides: Antimicrobial foldamers with heterogeneous backbones. J Am Chem Soc. 2004; 126(22):6848–6849. Lee EF, Sadowsky JD, Smith BJ, Czabotar PE, Peterson-Kaufman KJ, Colman PM, Gellman SH, Fairlie WD. Highresolution structural characterization of a helical α/β-peptide foldamer bound to the anti-apoptotic protein Bcl-xL. Angew Chem Int Edit. 2009; 48(24):4318–4322. Sadowsky JD, Schmitt MA, Lee H-S, Umezawa N, Wang S, Tomita Y, Gellman SH. Chimeric (α/β + α)-peptide ligands for the BH3-recognition cleft of Bcl-xL: Critical role of the molecular scaffold in protein surface recognition. J Am Chem Soc. 2005; 127(34):11966–11968. Sadowsky JD, Fairlie WD, Hadley EB, Lee H-S, Umezawa N, Nikolovska-Coleska Z, Wang S, Huang DCS, Tomita Y, Gellman SH. (α/β+α)-Peptide antagonists of BH3 domain/BclxL recognition: Toward general strategies for foldamer-based inhibition of proteinprotein interactions. J Am Chem Soc. 2007; 129(1):139–154. Koglin N, Zorn C, Beumer R, Cabrele C, Bubert C, Sewald N, Reiser O, Beck-Sickinger AG. Analogues of neuropeptide Y containing β-aminocyclopropane carboxylic acids are the shortest linear peptides that are selective for the Y1 receptor. Angew Chem Int Edit. 2003; 42(2):202–205. Baldauf C, Günther R, Hofmann H-J. Helix formation and folding in γ-peptides and their vinylogues. Helv Chim Acta. 2003; 86(7):2573–2588. Bouillère F, Thétiot-Laurent S, Kouklovsky C, Alezra V. Foldamers containing γ-amino acid residues or their analogues: structural features and applications. Amino Acids. 2011; 41(3):687–707. Karle IL, 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. 1997; 119(39):9087–9095. Araghi RR, Koksch B. A helix-forming αβγ-chimeric peptide with catalytic activity: A hybrid peptide ligase. Chem Commun. 2011; 47(12):3544–3546. Araghi RR, Jäckel C, Cölfen H, Salwiczek M, Völkel A, Wagner SC, Wieczorek S, Baldauf C, Koksch B. A β/γ motif to mimic α-helical turns in proteins. ChemBioChem. 2010; 11(3):335–339. Semetey V, Rognan D, Hemmerlin C, Graff R, Briand J-P, Marraud M, Guichard G. Stable helical secondary structure in short-chain N,N’-linked oligoureas bearing proteinogenic side chains. Angew Chem Int Edit. 2002; 41(11):1973–1975. Fischer L, Claudon P, Pendem N, Miclet E, Didierjean C, Ennifar E, Guichard G. The canonical helix of urea oligomers at atomic resolution: Insights into folding-induced axial organization. Angew Chem Int Edit. 2010; 112(6):1085–1088. Violette A, Fournel S, Lamour K, Chaloin O, Frisch B, Briand JP, Monteil H, Guichard G. Mimicking helical antibacterial peptides with nonpeptidic folding oligomers. Chem Biol. 2006; 13(5):531–538. Claudon P, Violette A, Lamour K, Decossas M, Fournel S, Heurtault B, Godet J, Mély Y, Jamart-Grégoire B, Averlant-Petit M-C, Briand J-P, Duportail G, Monteil H, Guichard G. Consequences of isostructural main-chain modifications for the design of antimicrobial foldamers: Helical mimics of hostdefense peptides based on a heterogeneous amide/urea backbone. Angew Chem Int Edit. 2010; 49(2):333–336.