Selection and characterization of a 7‐mer peptide binding to divalent cations |
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| Authors: | Daeyoung Han Seong Huh Heejoon Myung |
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| Affiliation: | 1. Department of Bioscience and Biotechnology, Hankuk University of Foreign Studies, Yong‐In, Gyung‐Gi Do 449‐791, Korea;2. Department of Chemistry, Hankuk University of Foreign Studies, Yong‐In, Gyung‐Gi Do 449‐791, Korea |
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| 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 Pb2+, Cd2+, Hg2+, and Cu2+. 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 Hg2+ 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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| Keywords: | phage display peptide divalent cation ITC Ala scanning mutant heavy metal binding |
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