Evaluation of a Cyclopentane-Based 纬-Amino Acid for the Ability to Promote 伪/纬-Peptide Secondary Structure

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• 作者：Michael W. Giuliano ; Stacy J. Maynard ; Aaron M. Almeida ; Andrew G. Reidenbach ; Li Guo ; Emily C. Ulrich ; Ilia A. Guzei ; Samuel H. Gellman
• 刊名：Journal of Organic Chemistry
• 出版年：2013
• 出版时间：December 20, 2013
• 年：2013
• 卷：78
• 期：24
• 页码：12351-12361
• 全文大小：596K
• 年卷期：v.78,no.24(December 20, 2013)
• ISSN：1520-6904

文摘

We report the asymmetric synthesis of the 纬-amino acid (1R,2R)-2-aminomethyl-1-cyclopentane carboxylic acid (AMCP) and an evaluation of this residue鈥檚 potential to promote secondary structure in 伪/纬-peptides. Simulated annealing calculations using NMR-derived distance restraints obtained for 伪/纬-peptides in chloroform reveal that AMCP-containing oligomers are conformationally flexible. However, additional evidence suggests that an internally hydrogen-bonded helical conformation is partially populated in solution. From these data, we propose characteristic NOE patterns for the formation of the 伪/纬-peptide 12/10-helix and discuss the apparent conformational frustration of AMCP-containing oligomers.