title: Selection and characterization of a 7-mer peptide binding to divalent cations.
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.
authors.affiliation: Department of Bioscience and Biotechnology, Hankuk University of Foreign Studies, Yong-In, Gyung-Gi Do 449-791, Korea.
authors.forename: Daeyoung
authors.initials: D
authors.lastname: Han
authors.forename: Seong
authors.initials: S
authors.lastname: Huh
authors.forename: Heejoon
authors.initials: H
authors.lastname: Myung
mesh_terms: D001665:Binding Sites; D002104:Cadmium / Q000737:chemistry*; D002151:Calorimetry; D002413:Cations, Divalent / Q000737:chemistry; D003300:Copper / Q000737:chemistry*; D007854:Lead / Q000737:chemistry*; D008628:Mercury / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*
chemical_list: D002413:Cations, Divalent; D010455:Peptides; D002104:Cadmium; D007854:Lead; D003300:Copper; D008628:Mercury