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Updated: May 19, 2026

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
Published on: October 9, 2021
The role of tryptophan spatial arrangement for antimicrobial-derived, membrane-active peptides adsorption and
Irina Schiopu1, Loredana Mereuta, Aurelia Apetrei
1Department of Physics, Laboratory of Molecular Biophysics and Medical Physics, Alexandru I. Cuza University, Iasi 700506, Romania.
Abstract:
Herein we explored the role of topological distribution of aromatic amino acids in peptide-membrane interfacial interactions. The membrane activity of closely related peptides and their binding energy is sensitive to the positioning of minimum two tryptophans, and by the degree of flanking at the membrane interface mediated by aromatic amino acids.
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