HWEI-YAN TSAI2026-10-162026-10-162005-01-01Pure ID: 14931641Pure UUID: 2863d83a-1f67-46ad-9207-9838d7e0613f10.1002/jccs.200500064https://www.scopus.com/pages/publications/33645411437https://scholars.csmu.edu.tw/handle/123456789/34010This article presents rotating ring-disc electrode investigations of (A=alanine, F=phenylalanine, G = glycine, L = leucine, W = tryptophan) W, GW, WGG, GWG, GGW, GWGG, and GGWA. In addition, the analyses of the copper complexes of the same peptides plus GF, FGG, GFG, FGG, GGFL, GGGG, AAAA, and GGGGGG have been carried out. The re suits suggest that an influential step in the reaction mechanism of the copper complexes of the tryptophan-containing peptides (W-peptides) is the alteration of the peptide structure after the one-electron oxidation of tryptophan. This change in structure leads to apositive shift in redox potential for the Cu(III)/Cu(II) couple. The analytical implications for the electro chemical detection of W-peptides as their copper complexes are applied for detection of W-containing bioactive peptides. Application of the optimized detection conditions of peptides as their Cu(II) complexes are as follows: (1) If sensitivity is paramount, detect the copper complexes at a relalively high potential, around 0.7 V vs. Ag/AgCl. (2) If selectivity is paramount, use a dual electrodedetector, oxidize at an up stream anode at 0.4 V, and detect at the downstream cathode at 0-0.1V.14enjournal article