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Updated: Mar 17, 2026

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
Published on: April 5, 2022
Interactions of α-Factor-1, a Yeast Pheromone, and Its Analogue with Copper(II) Ions and Low-Molecular-Weight Ligands
Karolina Bossak1, Mariusz Mital1,2, Jarosław Poznański1
1Institute of Biochemistry and Biophysics, Polish Academy of Sciences , Pawińskiego 5a, 02-106 Warsaw, Poland.
Abstract:
α-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, α-factor-1 and other XHX-type peptides are likely copper(II) carriers in biological systems.
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