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RESEARCH PRODUCT
Zinc Binding Sites Conserved in Short Neuropeptides Containing a Diphenylalanine Motif
Magdalena Rowinska-zyrekYifat MillerAleksandra HecelShira Ben-shushanHenryk KozłowskiHenryk Kozlowskisubject
Binding SitesZinc binding010405 organic chemistryStereochemistryPhenylalanineNeuropeptidesMolecular Conformationtechnology industry and agricultureSupramolecular chemistryNeuropeptideDipeptidesmacromolecular substancesMolecular Dynamics Simulation010402 general chemistry01 natural sciences0104 chemical sciencesInorganic ChemistryZincchemistry.chemical_compoundMotif (narrative)chemistryPhysical and Theoretical ChemistryDiphenylalaninedescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2019-12-07 | Inorganic Chemistry |