A study has been made of the interaction of Ni(II) and Co (II) ions with the following polypeptides: poly-(L)-lysine), poly-(L-ornithine), poly-(L-diaminobutyric acid) and poly-(L-histidine). It is shown that complexes involving amino nitrogens or deprotonated peptide nitrogens as ligands are formed at several pH values. Deprotonated peptide nitrogens participate in complex formation even in the case of physiological pH values, when a stable chelate system may be formed. When deprotonated peptide nitrogens in matrix backbones are involved in complex formation, no ordered structures is preserved in the complexes regions of a polypeptide. One may conclude from the results obtained that conformational properties of the polypeptides are strictly correlated to complex formation.
Interaction of polypeptides with metal ions
PALUMBO, MANLIO;
1979
Abstract
A study has been made of the interaction of Ni(II) and Co (II) ions with the following polypeptides: poly-(L)-lysine), poly-(L-ornithine), poly-(L-diaminobutyric acid) and poly-(L-histidine). It is shown that complexes involving amino nitrogens or deprotonated peptide nitrogens as ligands are formed at several pH values. Deprotonated peptide nitrogens participate in complex formation even in the case of physiological pH values, when a stable chelate system may be formed. When deprotonated peptide nitrogens in matrix backbones are involved in complex formation, no ordered structures is preserved in the complexes regions of a polypeptide. One may conclude from the results obtained that conformational properties of the polypeptides are strictly correlated to complex formation.Pubblicazioni consigliate
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