Arrangement of Proteinogenic alpha-Amino Acids on a Cyclic Peptide Comprising Alternate Biphenyl-Cored zeta-Amino Acids

作者：Tashiro Shohei^*; Chiba Masayuki; Shionoya Mitsuhiko^*

来源：Chemistry-An Asian Journal, 2017, 12(10): 1087-1094.

DOI：10.1002/asia.201700203

• amino acids
• biphenyl
• macrocycles
• NMR spectroscopy
• peptides

Aiming at precisely arranging several proteinogenic alpha-amino acids on a folded scaffold, we have developed a cyclic hexapeptide comprising an alternate sequence of biphenyl- cored zeta-amino acids and proteinogenic alpha-amino acids such as L-leucine. The amino acids were connected by typical peptide synthesis, and the resultant linear hexapeptide was intramolecularly cyclized to form a target cyclic peptide. Theoretical analyses and NMR spectroscopy suggested that the cyclic peptide was folded into an unsymmet-rical conformation, and the structure was likely to be flexible in CHCl3. The optical properties including UV/Vis absorption, fluorescence, and circular dichroism (CD) were also evaluated. Furthermore, the cyclic peptide became soluble in water by introducing three carboxylate groups at the periphery of the cyclic skeleton. This alpha/zeta-alternating cyclic peptide is therefore expected to serve as a unique scaffold for arranging several functionalities.

• 出版日期2017-5-18