cu(ii) and ni(ii) interactions with the terminally blocked hexapeptide ac-leu-ala-his-tyr-asn-lys-amide model of histone h2b (80–85)铜(ii)和镍(ii)与晚期的交互阻塞hexapeptide ac-leu-ala-his-tyr-asn-lys-amide模型组蛋白h2b(80 - 85).pdfVIP

Hindawi Publishing Corporation Bioinorganic Chemistry and Applications Volume 2008, Article ID 257038, 10 pages doi:10.1155/2008/257038 Research Article Cu(II) and Ni(II) Interactions with the Terminally Blocked Hexapeptide Ac-Leu-Ala-His-Tyr-Asn-Lys-amide Model of Histone H2B (80–85) Katerina Panagiotou,1 Maria Panagopoulou,1 Tilemachos Karavelas,1 Vassiliki Dokorou,1 Andrew Hagarman,2 Jonathan Soffer,2 Reinhard Schweitzer-Stenner,2 Gerasimos Malandrinos,1 and Nick Hadjiliadis1 1 Department of Chemistry, University of Ioannina, 45110 Ioannina, Greece 2 Department of Chemistry, Drexel University, 3141 Chestnut Street, Philadelphia, PA 19104, USA Correspondence should be addressed to Nick Hadjiliadis, nhadjis@uoi.gr Received 22 December 2007; Accepted 4 February 2008 Recommended by Imre Sovago The N- and C-terminal blocked hexapeptide Ac-Leu-Ala-His-Tyr-Asn-Lys-amide (LAHYNK) representing the 80–85 fragment of histone H2B was synthesized and its interactions with Cu(II) and Ni(II) ions were studied by potentiometric, UV-Vis, CD, EPR, and NMR spectroscopic techniques in solution. Our data reveal that the imidazole N(3) nitrogen atom is the primary ligating group for both metal ions. Sequential amide groups deprotonation and subsequent coordination to metal ions indicated an {Nimidazole , 3Namide } coordination mode above pH∼9, in all cases. In the case of Cu(II)-peptide system, the almost exclusive formation of the predominant species CuL in neutral media accounting for almost 98% of the total metal ion concentration at pH 7.3 strongly indicates that at physiological pH values the sequence -LAHYNK- of histone H2B provides very efficient binding sites for metal ions. The imidazole pyrrole N(1) ionization (but not coordination) was also detected in species CuH−4 L pres