整合生物学期刊网

应用天然产物 ›› 2018, Vol. 8 ›› Issue (1): 57-61.DOI: 10.1007/s13659-017-0150-x

• • 上一篇    下一篇

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

Quan Chi, Ying-Zhi Liu, Xian Wang   

  1. Key Laboratory of Analytical Chemistry of the State Ethnic Affairs Commission, College of Chemistry and Materials Science, South-Central University for Nationalities, Wuhan, Hubei 430074, People's Republic of China
  • 收稿日期:2017-11-13 修回日期:2017-12-13 出版日期:2018-02-24 发布日期:2018-02-27
  • 基金资助:
    This research was supported by the National Natural Science Foundation of China (Grant No. 21675176), the Natural Science Foundation of Hubei Province (Grant No. 2014CFA025), and 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.

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

Quan Chi, Ying-Zhi Liu, Xian Wang   

  1. Key Laboratory of Analytical Chemistry of the State Ethnic Affairs Commission, College of Chemistry and Materials Science, South-Central University for Nationalities, Wuhan, Hubei 430074, People's Republic of China
  • Received:2017-11-13 Revised:2017-12-13 Online:2018-02-24 Published:2018-02-27
  • Contact: Xian Wang

摘要: Noncovalent interactions between ligands and targeting proteins are essential for understanding molecular mechanisms of proteins. In 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 observed. The corresponding association constants were calculated according to the deconvoluted spectra. The order of the relative binding affinities of the selected oligosaccharides with Cyt c were as Mal Ⅲ > Mal IV > Mal Ⅱ > Mal V > Mal VI > Mal VⅡ. The results indicated that the stability of noncovalent protein complexes was intimately correlated to the molecular structure of bound ligand. The 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 complexes. In addition, the steric structure of ligand was also critical for an appropriate interaction with the binding pocket of proteins.

关键词: Electrospray ionization mass spectrometry, Maltoligosaccharides, Cytochrome c complexes, Structure-binding relationship

Abstract: Noncovalent interactions between ligands and targeting proteins are essential for understanding molecular mechanisms of proteins. In 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 observed. The corresponding association constants were calculated according to the deconvoluted spectra. The order of the relative binding affinities of the selected oligosaccharides with Cyt c were as Mal Ⅲ > Mal IV > Mal Ⅱ > Mal V > Mal VI > Mal VⅡ. The results indicated that the stability of noncovalent protein complexes was intimately correlated to the molecular structure of bound ligand. The 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 complexes. In addition, the steric structure of ligand was also critical for an appropriate interaction with the binding pocket of proteins.

Key words: Electrospray ionization mass spectrometry, Maltoligosaccharides, Cytochrome c complexes, Structure-binding relationship