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Zinc Complexes of Amino Acids and Peptides, 8[ ]. Difunctional Dipeptides Containing Cysteine or Histidine: Solution Behavior and Zinc Complextion
Author(s) -
Gockel Peter,
Vahrenkamp Heinrich
Publication year - 1996
Publication title -
chemische berichte
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 0009-2940
DOI - 10.1002/cber.19961291016
Subject(s) - chemistry , histidine , zinc , cysteine , imidazole , amino acid , potentiometric titration , chelation , stereochemistry , medicinal chemistry , peptide , polymer chemistry , organic chemistry , biochemistry , ion , enzyme
The dipeptides Ac–Cys–Val–OH ( 1a ) and Ac–His–Val–OH ( 1b ), H–Gly–Cys–OEt ( 2a ) and H–Val–His–OEt ( 2b ) as well as Z–Asp–Cys–OH ( 3a ) and Z–Asp–His–OH ( 3b ) (Z = benzyloxycarbonyl) were prepared, and their zinc complexation was investigated by potentiometric methods. They have in common that in addition to the cysteine thiolate or the histidine imidazole the second amino acid offers one donor function. The complex stabilities are very close to those of the corresponding difunctional derivatives of the single amino acids cysteine or histidine. This indicates the presence of seven‐ to ten‐membered chelate rings.