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Can the alpha-hydroxymethylated amino acid residue influence the peptide binding ability towards copper(II) ions?

Lodyga-Chruscinska, Elzbieta and Micera, Giovanni and Sanna, Daniele and Kozlowski, Henryk and Kaczmarek, Krzysztof and Olejnik, Jadwiga and Leplawy, Miroslaw T. (1998) Can the alpha-hydroxymethylated amino acid residue influence the peptide binding ability towards copper(II) ions? Journal of Inorganic Biochemistry, Vol. 72 (3-4), p. 187-194. ISSN 0162-0134. Article.

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DOI: 10.1016/S0162-0134(98)10079-X


Complexing ability of tetrapeptides Phe– (R,S)HmR–Arg–Lys, Phe–(R)HmR–Arg–Lys and Phe–(R,S)HmO–Arg–Lys containing potential multi-donor systems provided by the novel amino acid α-hydroxymethylarginine or by α-hydroxymethylornithine has been investigated by potentiometry and the spectroscopic methods (EPR, UV-VIS and CD). Their complexes with copper(II) ions were compared with those of the parent peptides Phe–Ala–Ala–Lys, Phe–Ser–Ala–Lys, Phe–Arg–Arg–Lys and Phe–Orn–Arg–Lys. The significant enhancement of thermodynamic stability is observed for the 2N and 3N species. The CD and EPR spectra support square-planar geometry in 3N species formed at physiological pH. The distortion of the metal environment is induced through the bend conformation adopted by the peptide molecule. The Lys residue is the critical factor influencing this geometry distortion in the 3N species. However, the presence of a α-hydroxymethyl group affects the stability of the complexes, most likely by stabilizing conformations suitable for metal complexation.

Item Type:Article
ID Code:1437
Uncontrolled Keywords:Α-Hydroxymethylated peptide complexes, α-Hydroxymethylornithine, α-Hydroxymethylarginine
Subjects:Area 03 - Scienze chimiche > CHIM/03 Chimica generale e inorganica
Divisions:001 Università di Sassari > 01 Dipartimenti > Chimica
002 Altri enti e centri di ricerca del Nord Sardegna > CNR-Consiglio Nazionale delle Ricerche > Istituto di chimica biomolecolare, Sassari
Publisher:Elsevier Science
Additional Information:Pubblicato online il 17 febbraio 1999.
Deposited On:18 Aug 2009 10:05

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