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Zinc binding sites conserved in short neuropeptides containing a diphenylalanine motif.
Autorzy
Rok wydania
2020
Czasopismo
Numer woluminu
59
Strony
925-929
DOI
10.1021/acs.inorgchem.9b03199
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
A diphenylalanine motif in peptides plays a crucial role in supramolecular systems. The current work represents a novel strategy in which a diphenylalanine motif in the central domain of neuropeptides conserves the specific Zn2+ binding site and prevents "hopping" of the Zn2+ ion between alternative metal binding sites. Alternative metal binding sites may also include carboxylic atoms in the terminal domains of a peptide. Therefore, one needs to design a peptide in which the metal will not bind the carboxylic groups in the terminal domains. Herein, we propose that engineering and designing peptides with a diphenylalanine motif in the central domain may yield excellent metal chelators.
Słowa kluczowe
Peptides and proteins, Metals, Ions, Chemical structure, Conformation
Adres publiczny
http://dx.doi.org/10.1021/acs.inorgchem.9b03199
Strona internetowa wydawcy
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