Analysis of the binding sites with NL-101 to amino acids and peptides by HPLC/MS/MS

作     者：Lingzi Dai Nian Guo Yaqin Liu Shanshan Shen Qiufu Ge Yuanjiang Pan 

作者机构：Department of Chemistry Zhejiang University Hangzhou Pharmaceutical Group Co. Ltd. 

出 版 物：《Chinese Chemical Letters》 (中国化学快报（英文版）)

年 卷 期：2019年第30卷第1期

页      面：103-106页

核心收录：

学科分类：07[理学] 0703[理学-化学] 

基　　金：supported by the National Natural Science Foundation of China (Nos. 21327010  21372199) 

主　　题：High-performance liquid chromatography/ tandem mass spectrometry NL-101 Amino acids Peptides Binding sites 

摘      要：The binding between NL-101, a novel nitrogen mustard anti-cancer drug, with amino acids and peptides has been investigated by high performance liquid chromatography electrospray tandem mass spectrometry(HPLC/ESI-MS/MS). This study offers supporting data of the interaction among drug and amino acids and peptides, which could potentially explain the cytotoxic and mutagenic effects of the drug. Collision-induced dissociation(CID) experiment demonstrated that under the same collision energy, the amino group combined with NL-101 adducts are sensitive and often produce more fragment ions; the carboxyl group combined with NL-101 adducts are hard to break and display fewer fragment ions. In addition, when other group(like sulfhydryl group) of amino acids binds to NL-101, CID spectra show different fragmentation pattern. These differences could display structural information about the drug adducts and be utilized as location of the authentic binding sites.