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Copper (II) Complexes with Ac-HXH-NHMe (X=Gly, Ala and Aib) Peptide Motifs: Influence of Increasing CH3 Groups at Cα of Residue X on the Coordination in Solution

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The interaction of Cu(II) ion with small peptides has been an interesting subject to clarify the role of copper in detail. As various Cu(II)-oligopeptide complexes can also be good models for the active centers of metalloenzymes, complexes of tripeptide and tetrapeptides are frequently investigated instead of the complexes of large peptides. The histidine side-chains of various metalloproteins frequently take part in the copper(II) coordination. Accordingly, we studied the coordination of Cu(II) to the N and C terminal protected tripeptide ligands LA (Ac-HisGlyHis-NHMe), LB (Ac-HisAlaHis- NHMe) and LC (Ac-HisAibHis-NHMe) in aqueous solution potentiometrially in order to determine the effect of Cα methyl groups at middle residue acid on the ligation of the backbone NH and also on histidine's Nim of coordination. Species distribution curves indicates that in acidic pH, all three peptides behave as bidentate ligands and a macrochelate forms on the metal coordination with the two histidine imidazolyl N. This coordination remains unaffected with the +I effect of increasing CH3 groups at Cα of middle residue. In the pH range 4-8, the tridentate coordination from the peptide is seen in ligand LA and LB while it is absent in LC due to +I effect of two Cα methyl groups at middle residue as they makes Nterminal NH deprotonation difficult in this pH range and it takes place along with C terminal NH and only 4N coordinated species formed at higher pH. These 4N (Nim, N-, N-, Nim) coordinated species are formed by all the three ligands at higher pH values.

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Keywords: Protonation; carbonyl oxygen; deprotonated amide group; peptide ligands; potentiometric method

Document Type: Research Article

Affiliations: Department of Chemistry,Indian Institute of Technology Roorkee, Roorkee - 247 667, India.

Publication date: 2007-04-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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