Wydział Chemii

Maria Antonietta Zoroddu

Teresa Kowalik-Jankowska

Henryk Kozłowski

Konstantin Salnikow

Max Costa

2001

Journal of Inorganic Biochemistry

85

47-54

10.1016/S0162-0134(00)00204-X

Naukowa

Angielski

Artykuł

The tetradecapeptide containing the 10 aminoacid repeated sequence on the C-terminus of the Ni(II)-induced Cap43 protein, was analyzed for Ni(II) and Cu(II) binding. A combined pH-metric and spectroscopic UV–VIS, EPR, CD and NMR study of Ni(II) and Cu(II) binding to the blocked CH₃CO-Thr-Arg-Ser-Arg-Ser-His-Thr-Ser-Glu-Gly-Thr-Arg-Ser-Arg-NH₂ (Ac-TRSRSHTSEGTRSR-Am) peptide, modeling a part of the C-terminal sequence of the Cap43 protein, revealed the formation of octahedral complexes involving imidazole nitrogen of histidine, at pH 5.5 and pH 7 for Cu(II) and Ni(II), respectively; a major square planar 4N–Ni(II) complex (about 100% at pH 9, log K*=−28.16) involving imidazole nitrogen of histidine and three deprotonated amide nitrogens of the backbone of the peptide was revealed; a 3N–Cu(II) complex (maximum about 70% at pH 7, log K*=−13.91) and a series of 4N–Cu(II) complexes starting at pH 5.5 (maximum about 90% at pH 8.7, log K*=−21.39 for CuH₋₃L), were revealed. This work supports the existence of a metal binding site at the COOH-terminal part of the Cap43 peptide.

Ni(II), Cu(II), Bindi, 14-aminoacid peptide

https://doi.org/10.1016/S0162-0134(00)00204-X

http://www.elsevier.com