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Selection and characterization of a 7-mer peptide binding to divalent cations

✍ Scribed by Daeyoung Han; Seong Huh; Heejoon Myung

Publisher
John Wiley and Sons
Year
2011
Tongue
English
Weight
192 KB
Volume
17
Category
Article
ISSN
1075-2617

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✦ Synopsis

Abstract

A 7‐mer peptide (S‐T‐L‐P‐L‐P‐P) that bound to various divalent cations was selected from a phage display peptide library. Isothermal calorimetric analysis revealed that the peptide bound to Pb^2+^, Cd^2+^, Hg^2+^, and Cu^2+^. Through the use of CD studies, no secondary structural changes were observed for the peptide upon binding to divalent cations. Ala scanning mutant peptides bound to Hg^2+^ with a reduced affinity. However, no single substitution was shown to affect the overall affinity. We suggest that Pro residues chelate divalent cations, while the structure formed by the peptide is also important for the binding process. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.

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