
Yifat Miller
Senior Academic
Zinc Binding Sites Conserved in Short Neuropeptides Containing a Diphenylalanine Motif
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.
| Publication language | English |
| Pages | 925-929 |
| Journal | Inorganic Chemistry |
| Volume | 59 |
| Issue number | 1 |
| Publication status | Published - 06.01.2020 |
ASJC Scopus subject areas
Physical and Theoretical Chemistry
Inorganic Chemistry