Controlling the Helix Handedness of ααβ-Peptide Foldamers through Sequence Shifting

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• 作者：Dr. Monika Szefczyk ; Dr. Ewelina Węglarz-Tomczak ; Paulina Fortuna ; Agnieszka Krzysztoń ; Dr. Ewa Rudzińska-Szostak and Dr. Łukasz Berlicki
• 刊名：Angewandte Chemie
• 出版年：2017
• 出版时间：February 13, 2017
• 年：2017
• 卷：129
• 期：8
• 页码：2119-2123
• 全文大小：1967K
• ISSN：1521-3757

文摘

Peptide foldamers containing both cis-β-aminocyclopentanecarboxylic acid and α-amino acid residues combined in various sequence patterns (ααβ, αααβ, αβααβ, and ααβαααβ) were screened using CD and NMR spectroscopy for the tendency to form helices. ααβ-Peptides were found to fold into an unprecedented and well-defined 16/17/15/18/14/17-helix. By extending the length of the sequence or shifting a fragment of the sequence from one terminus to another in ααβ-peptides, the balance between left-handed and right-handed helix populations present in the solution can be controlled. Engineering of the peptide sequence could lead to compounds with either a strong propensity for the selected helix sense or a mixture of helical conformations of opposite senses.