Study on the Structural Effect of Maltoligosaccharides on Cytochrome c Complexes Stabilities by Native Mass Spectrometry

作     者：Quan Chi Ying-Zhi Liu Xian Wang 

作者机构：Key Laboratory of Analytical Chemistry of the State Ethnic Affairs CommissionCollege of Chemistry and Materials ScienceSouth-Central University for NationalitiesWuhanHubei 430074People’s Republic of China 

出 版 物：《Natural Products and Bioprospecting》 (应用天然产物（英文）)

年 卷 期：2018年第8卷第1期

页      面：57-61页

学科分类：081704[工学-应用化学] 07[理学] 08[工学] 070303[理学-有机化学] 0710[理学-生物学] 0832[工学-食品科学与工程（可授工学、农学学位）] 1007[医学-药学(可授医学、理学学位)] 1004[医学-公共卫生与预防医学(可授医学、理学学位)] 1002[医学-临床医学] 1001[医学-基础医学(可授医学、理学学位)] 0817[工学-化学工程与技术] 0703[理学-化学] 0901[农学-作物学] 0902[农学-园艺学] 

基　　金：supported by the National Natural Science Foundation of China(Grant No.21675176) the Natural Science Foundation of Hubei Province(Grant No.2014CFA025) the Preferred Research Foundation for the Returned Overseas Scholars from Ministry of Human Resources and Social Security of the People’s Republic of China(Grant No.BZY14036)for financial supports 

主　　题：Electrospray ionization mass spectrometry Maltoligosaccharides Cytochrome c complexes Structure-binding relationship 

摘      要：Noncovalent interactions between ligands and targeting proteins are essential for understanding molecular mechanisms of *** this work,we investigated the interaction of Cytochrome c(Cyt c)with maltoligosaccharides,namely maltose(Mal Ⅱ),maltotriose(Mal Ⅲ),maltotetraose(Mal Ⅳ),maltopentaose(Mal Ⅴ),maltohexaose(Mal Ⅵ)and maltoheptaose(Mal Ⅶ).Using electrospray ionization mass spetrometry(ESI-MS)assay,the 1:1 and 1:2 complexes formed by Cyt c with maltoligosaccharide ligand were *** corresponding association constants were calculated according to the deconvoluted *** order of the relative binding affinities of the selected oligosaccharides with Cyt c were as MalⅢMalⅣMalⅡMalⅤMalⅥMalⅦ.The results indicated that the stability of noncovalent protein complexes was intimately correlated to the molecular structure of bound *** relevant functional groups that could form H-bonds,electrostatic or hydrophobic forces with protein’s amino residues played an important role for the stability of protein *** addition,the steric structure of ligand was also critical for an appropriate interaction with the binding pocket of proteins.