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

查看全文 作  者:Lingzi [1]Dai;Nian [1]Guo;Yaqin [1]Liu;Shanshan [1]Shen;Qiufu [2]Ge;Yuanjiang [1]Pan 高影响力作者 机构地区:[1]Department of Chemistry, Zhejiang University;[2]Hangzhou Pharmaceutical Group Co., Ltd.高影响力机构 出  处:《Chinese Chemical Letters》索引2019年第30卷第1期,共4页高影响力期刊 基  金:supported by the National Natural Science Foundation of China (Nos. 21327010, 21372199) 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. 关 键 词:High-performance liquid chromatography/ TANDEM mass SPECTROMETRY NL-101 AMINO ACIDS PEPTIDES Binding sites
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