| ORIGINAL ARTICLES |
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Study on the Structural Effect of Maltoligosaccharides on Cytochrome c Complexes Stabilities by Native Mass Spectrometry |
| Quan Chi, Ying-Zhi Liu, Xian Wang |
| 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 |
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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.
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Electrospray ionization mass spectrometry
Maltoligosaccharides
Cytochrome c complexes
Structure-binding relationship
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Corresponding Authors:
Xian Wang
E-mail: xwang27@hotmail.com
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Issue Date: 27 February 2018
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