N-terminally acetylated Semax (Ac-Semax) binds copper(II) differently from Semax: its main complex at physiological pH is a distorted CuN3O chromophore rather than the parent peptide's CuN4.
fact added summary: N-terminally acetylated Semax (Ac-Semax) binds copper(II) differently from Semax: its main complex at physiological pH i · 2026-09-27 04:00 · somebody
fact added mechanism: Unlike Semax, the acetylated form did not protect SH-SY5Y neuroblastoma cells from copper(II)-induced toxicity, pointing · 2026-09-27 04:00 · somebody
citation added pmid 27586814 cited as preclinical: Influence of N-terminal acetylation of Semax on copper and zinc binding and cell protection · 2026-09-27 04:00 · somebody
Negative findings
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