Crystal structures of peptidic catalysts of the H-dPro-Pro-Xaa type

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• 作者：Claudio E. Grü ; nenfelder ; Jessica K. Kisunzu ; Nils Trapp ; Robert Kastl and Helma Wennemers
• 刊名：Peptide Science
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：108
• 期：1
• 全文大小：864K
• ISSN：1097-0282a

文摘

Crystal structures of catalytically active tripeptides of the general type H-dPro-Pro-Xaa and related N-acetylated analogs were compared. The influence of acylation at the N-terminus, the nature of the C-terminal residue, coordinating groups, and intramolecular hydrogen bonds on the conformation of the tripeptides was examined. Regardless of the presence or absence of stabilizing intramolecular H-bonds or n → π* interactions, all of the analyzed peptides share a β-turn-like conformation, which highlights the structural rigidity of the dPro-Pro motif and its value for conformational preorganization. The C-terminal residues and coordinating moieties were found to affect the turn-conformation, which suggests that H-dPro-Pro-Xaa type peptides are sufficiently flexible to adopt distinctly different but related conformations.