Study on the Structural Effect of Maltoligosaccharides on Cytochrome c Complexes Stabilities by Native Mass Spectrometry
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 (M...
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| Format: | Article |
| Language: | English |
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SpringerOpen
2018-01-01
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| Series: | Natural Products and Bioprospecting |
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| Online Access: | http://link.springer.com/article/10.1007/s13659-017-0150-x |
| _version_ | 1818067813635457024 |
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| author | Quan Chi Ying-Zhi Liu Xian Wang |
| author_facet | Quan Chi Ying-Zhi Liu Xian Wang |
| author_sort | Quan Chi |
| collection | DOAJ |
| description | 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. Graphical Abstract |
| first_indexed | 2024-12-10T15:29:39Z |
| format | Article |
| id | doaj.art-3742367664434d029d70cc111e83f73e |
| institution | Directory Open Access Journal |
| issn | 2192-2195 2192-2209 |
| language | English |
| last_indexed | 2024-12-10T15:29:39Z |
| publishDate | 2018-01-01 |
| publisher | SpringerOpen |
| record_format | Article |
| series | Natural Products and Bioprospecting |
| spelling | doaj.art-3742367664434d029d70cc111e83f73e2022-12-22T01:43:26ZengSpringerOpenNatural Products and Bioprospecting2192-21952192-22092018-01-0181576110.1007/s13659-017-0150-xStudy on the Structural Effect of Maltoligosaccharides on Cytochrome c Complexes Stabilities by Native Mass SpectrometryQuan Chi0Ying-Zhi Liu1Xian Wang2Key Laboratory of Analytical Chemistry of the State Ethnic Affairs Commission, College of Chemistry and Materials Science, South-Central University for NationalitiesKey Laboratory of Analytical Chemistry of the State Ethnic Affairs Commission, College of Chemistry and Materials Science, South-Central University for NationalitiesKey Laboratory of Analytical Chemistry of the State Ethnic Affairs Commission, College of Chemistry and Materials Science, South-Central University for NationalitiesAbstract 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. Graphical Abstracthttp://link.springer.com/article/10.1007/s13659-017-0150-xElectrospray ionization mass spectrometryMaltoligosaccharidesCytochrome c complexesStructure-binding relationship |
| spellingShingle | Quan Chi Ying-Zhi Liu Xian Wang Study on the Structural Effect of Maltoligosaccharides on Cytochrome c Complexes Stabilities by Native Mass Spectrometry Natural Products and Bioprospecting Electrospray ionization mass spectrometry Maltoligosaccharides Cytochrome c complexes Structure-binding relationship |
| title | Study on the Structural Effect of Maltoligosaccharides on Cytochrome c Complexes Stabilities by Native Mass Spectrometry |
| title_full | Study on the Structural Effect of Maltoligosaccharides on Cytochrome c Complexes Stabilities by Native Mass Spectrometry |
| title_fullStr | Study on the Structural Effect of Maltoligosaccharides on Cytochrome c Complexes Stabilities by Native Mass Spectrometry |
| title_full_unstemmed | Study on the Structural Effect of Maltoligosaccharides on Cytochrome c Complexes Stabilities by Native Mass Spectrometry |
| title_short | Study on the Structural Effect of Maltoligosaccharides on Cytochrome c Complexes Stabilities by Native Mass Spectrometry |
| title_sort | study on the structural effect of maltoligosaccharides on cytochrome c complexes stabilities by native mass spectrometry |
| topic | Electrospray ionization mass spectrometry Maltoligosaccharides Cytochrome c complexes Structure-binding relationship |
| url | http://link.springer.com/article/10.1007/s13659-017-0150-x |
| work_keys_str_mv | AT quanchi studyonthestructuraleffectofmaltoligosaccharidesoncytochromeccomplexesstabilitiesbynativemassspectrometry AT yingzhiliu studyonthestructuraleffectofmaltoligosaccharidesoncytochromeccomplexesstabilitiesbynativemassspectrometry AT xianwang studyonthestructuraleffectofmaltoligosaccharidesoncytochromeccomplexesstabilitiesbynativemassspectrometry |