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Updated: Jan 2, 2026

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
Published on: January 26, 2024
Zinc Binding Sites Conserved in Short Neuropeptides Containing a Diphenylalanine Motif
Shira Ben-Shushan, Aleksandra Hecel1, Magdalena Rowinska-Zyrek1
1Faculty of Chemistry , University of Wroclaw , Joliot-Curie 14 , Wroclaw 50-383 , Poland.
Abstract:
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.
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