Braun K P, Cody R B, Jones D R, Peterson C M
Sansum Medical Research Foundation, Santa Barbara, California 93105, USA.
J Biol Chem. 1995 May 12;270(19):11263-6. doi: 10.1074/jbc.270.19.11263.
Acetaldehyde is the first oxidation product of ethanol in vivo. Lysine residues in proteins such as hemoglobin have been implicated as target structures for acetaldehyde adducts resulting from ethanol consumption. Although the presence of both stable and unstable acetaldehyde-hemoglobin adducts has been established, the structural characterization of the adducts has received relatively little attention. As a model for such adduct formation, we studied the peptide pentalysine in vitro. Pentalysine has several potential sites for adduct formation. The amino-terminal amine group as well as the epsilon-amine groups of each lysine side chain can serve as potential sites for modification by acetaldehyde. Mass spectrometry, nuclear magnetic resonance, and Raman spectroscopy were employed to demonstrate that acetaldehyde forms a stable linkage to lysine amine groups via a Schiff base.
乙醛是乙醇在体内的首个氧化产物。诸如血红蛋白等蛋白质中的赖氨酸残基被认为是因摄入乙醇而形成的乙醛加合物的靶标结构。尽管已经证实了稳定和不稳定的乙醛 - 血红蛋白加合物的存在，但加合物的结构表征受到的关注相对较少。作为此类加合物形成的模型，我们在体外研究了五聚赖氨酸肽。五聚赖氨酸有几个潜在的加合物形成位点。每个赖氨酸侧链的氨基末端胺基以及ε - 胺基都可作为乙醛修饰的潜在位点。采用质谱、核磁共振和拉曼光谱来证明乙醛通过席夫碱与赖氨酸胺基形成稳定的连接。
