| Title: | "Interactions of alpha-Factor-1, a Yeast Pheromone, and Its Analogue with Copper(II) Ions and Low-Molecular-Weight Ligands Yield Very Stable Complexes" |
| Author(s): | Bossak K; Mital M; Poznanski J; Bonna A; Drew S; Bal W; |
| Address: | "Institute of Biochemistry and Biophysics, Polish Academy of Sciences , Pawinskiego 5a, 02-106 Warsaw, Poland. Florey Department of Neuroscience and Mental Health, The University of Melbourne , Melbourne, Victoria 3010, Australia" |
| DOI: | 10.1021/acs.inorgchem.6b01441 |
| ISSN/ISBN: | 1520-510X (Electronic) 0020-1669 (Linking) |
| Abstract: | "alpha-Factor-1 (WHWLQLKPGQPMY), a peptidic pheromone of Saccharomyces cerevisiae yeast, contains a XHX type copper(II) binding N-terminal site. Using a soluble analogue, WHWSKNR-amide, we demonstrated that the W(1)H(2)W(3) site alone binds copper(II) with a Kd value of 0.18 pM at pH 7.4 and also binds imidazole (Im) in a ternary complex (Kd of 1 mM at pH 7.4). This interaction boosts the ability of the peptide to sequester copper(II) depending on the Im concentration up to a subfemtomolar range, not available for any oligopeptidic system studied before. Therefore, alpha-factor-1 and other XHX-type peptides are likely copper(II) carriers in biological systems" |
| Keywords: | "Amides/chemistry Binding Sites Circular Dichroism Copper/*metabolism Imidazoles/chemistry/metabolism Ligands Mating Factor/*chemistry/*metabolism Protein Conformation Spectrophotometry, Ultraviolet;neuroscience;" |
| Notes: | "MedlineBossak, Karolina Mital, Mariusz Poznanski, Jaroslaw Bonna, Arkadiusz Drew, Simon Bal, Wojciech eng 2016/08/02 Inorg Chem. 2016 Aug 15; 55(16):7829-31. doi: 10.1021/acs.inorgchem.6b01441. Epub 2016 Aug 1" |
