alpha-Helical Structures of Oligopeptides with an Alternating L-Leu-Aib Segment

作者：Demizu Yosuke^*; Okitsu Koyo; Yamashita Hiroko; Doi Mitsunobu; Misawa Takashi; Oba Makoto; Tanaka Masakazu; Kurihara Masaaki^*

来源：European Journal of Organic Chemistry, 2016, 2016(16): 2815-2820.

DOI：10.1002/ejoc.201600327

• Helical structures
• Conformation analysis
• Amino acids
• Peptides
• Oligopeptides
• Protein folding

We investigated the preferred conformations of L-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, hexapeptide 3 forms a (P) 3(10)-helix, and octapeptide 4 and decapeptide 5 form (P) alpha-helices as their preferred conformations in solution. In the crystalline state, both octapeptide 4 and decapeptide 5 fold into (P) alpha-helices.

• 出版日期2016-6