Α‐Helical Structures of Oligopeptides with an Alternating l‐Leu‐Aib Segment. Issue 16 (20th May 2016)

• Record Type: Journal Article
• Authors: Demizu, Yosuke; Okitsu, Koyo; Yamashita, Hiroko; Doi, Mitsunobu; Misawa, Takashi; Oba, Makoto; Tanaka, Masakazu; Kurihara, Masaaki
• Is Part Of: European journal of organic chemistry. Issue 16(2016)
• Page Start: 2815
• Page End: 2820
• Publication Date: 2016-05-20
• Subjects: Helical structures -- Conformation analysis -- Amino acids -- Peptides -- Oligopeptides -- Protein folding; Chemistry, Organic -- Periodicals; Organic compounds -- Synthesis -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1002/ejoc.201600327
• Languages: English
• ISSNs: 1434-193X

Abstract

Abstract : We investigated the preferred conformations ofl ‐Leu‐Aib‐alternating peptides, Boc‐(l ‐Leu‐Aib) n ‐OMe ( n = 1:1, 2:2, 3:3, 4:4, 5:5 ), in solution and in the crystalline state. Peptides that contain more than six amino acid residues fold into right‐handed ( P ) helical structures. Specifically, hexapeptide3 forms a ( P ) 310 ‐helix, and octapeptide4 and decapeptide5 form ( P ) α‐helices as their preferred conformations in solution. In the crystalline state, both octapeptide4 and decapeptide5 fold into ( P ) α‐helices. Abstract : Repeating dipeptidel ‐Leu‐Aib segments have greater α‐helix‐inducing potential than repeating tripeptidel ‐Leu‐l ‐Leu‐Aib segments.