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Selection and characterization of a 7‐mer peptide binding to divalent cations
Author(s) -
Han Daeyoung,
Huh Seong,
Myung Heejoon
Publication year - 2011
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1374
Subject(s) - divalent , peptide , chemistry , chelation , stereochemistry , isothermal titration calorimetry , divalent metal , crystallography , biochemistry , inorganic chemistry , organic chemistry , metal
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.