Complex Formation and Hydrolytic Processes of Protected Peptides Containing the -SXH- Motif in the Presence of Nickel(II) Ion.
Chembiochem
; : e202400475, 2024 Jul 12.
Article
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| MEDLINE
| ID: mdl-39001608
ABSTRACT
Interactions between metal ions and proteins are considered reversible, such as the coordination of a metal ion to a protein or enzyme, but irreversible processes like the oxidative reactions, aggregation or hydrolytic processes may occur. In the presence of Ni(II)-ions selective hydrolysis of the peptides containing the -SXH- or -TXH- motif was observed. Since the side chain of histidine serves as the metal ion binding site for many native proteins, and very often histidine is present in a -SXH- or -TXH- sequence, to study the complex formation and hydrolytic processes in presence of nickel(II) ion four peptides were synthesised Ac-SKHM-NH2, A3SSH-NH2, A4SSH-NH2, AAAeKSH-NH2. The Ni(II)-induced hydrolysis of Ac-SKHM-NH2 peptide occurs rapidly in alkaline medium already at room temperature. In two peptides containing -SSH- sequence on the C-termini, the N-terminal part is the major binding site for the nickel(II) ion, but the formation of dinuclear complexes was also observed. In the [Ni2LH-6]2- complex of hexapeptide, the coordination sphere of the metal ions is saturated with deprotonated Ser-O-, which does not result in hydrolysis of the peptide. For A4SSH-NH2, both Ni(II) ions fulfill the conditions for hydrolysis, which was confirmed by HPLC analyses at pH ~ 8.2 and 25 °C.
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MEDLINE
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En
Revista:
Chembiochem
Asunto de la revista:
BIOQUIMICA
Año:
2024
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Article