人血清白蛋白
脂肪酸
化学
肽
生物化学
酰化
油酸
棕榈酸
结合位点
白蛋白
血浆蛋白结合
血清白蛋白
脂肪酸结合蛋白
立体化学
基因
催化作用
作者
Haitao Hu,Anthony S. Ransdell,Hongchang Qu,Jim D. Durbin,Francisco A. Valenzuela,Selene Hernandez-Buquer,Malgorzata D. Gonciarz
标识
DOI:10.1021/acschembio.3c00018
摘要
Peptides represent an increasingly important class of pharmaceutical products. During the last decade or so, acylation with fatty acids has demonstrated considerable success in prolonging the circulating half-life of therapeutic peptides by exploiting the ability of fatty acids to reversibly bind to human serum albumin (HSA), thus significantly impacting their pharmacological profiles. Employing methyl-13C-labeled oleic acid or palmitic acid as probe molecules and exploiting HSA mutants designed to probe fatty acid binding, the signals in two-dimensional (2D) nuclear magnetic resonance (NMR) spectra corresponding to high-affinity fatty acid binding sites in HSA were assigned. Subsequently, using a set of selected acylated peptides, competitive displacement experiments by 2D NMR identified a primary fatty acid binding site in HSA utilized in acylated peptide binding. These results represent an important first step toward understanding the structural basis for acylated peptides binding to HSA.
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