The Mechanism Underlying the Amylose-Zein Complexation Process and the Stability of the Molecular Conformation of Amylose-Zein Complexes in Water Based on Molecular Dynamics Simulation
The aim of this study was to employ molecular dynamics simulations to elucidate the mechanism involved in amylose–zein complexation and the stability of the molecular conformation of amylose–zein complexes in water at the atomic and molecular levels. The average root mean square deviation and radius...
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MDPI AG
2023-03-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/12/7/1418 |
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| author | Chaofan Wang Na Ji Lei Dai Yang Qin Rui Shi Liu Xiong Qingjie Sun |
| author_facet | Chaofan Wang Na Ji Lei Dai Yang Qin Rui Shi Liu Xiong Qingjie Sun |
| author_sort | Chaofan Wang |
| collection | DOAJ |
| description | The aim of this study was to employ molecular dynamics simulations to elucidate the mechanism involved in amylose–zein complexation and the stability of the molecular conformation of amylose–zein complexes in water at the atomic and molecular levels. The average root mean square deviation and radius of gyration were lower for amylose–zein complexes (1.11 nm and 1 nm, respectively) than for amylose (2.13 nm and 1.2 nm, respectively), suggesting a significantly higher conformational stability for amylose–zein complexes than for amylose in water. The results of radial distribution function, solvent-accessible surface area, and intramolecular and intermolecular hydrogen bonds revealed that the amylose–zein interaction inhibited water permeation into the amylose cavity, leading to enhanced conformational stabilities of the V-type helical structure of amylose and the amylose–zein complexes. Furthermore, the amylose in amylose–zein complexes displayed the thermodynamically stable <sup>4</sup>C<sub>1</sub> conformation. These findings can provide theoretical guidance in terms of the application of protein on starch processing aiming to improve the physicochemical and functional properties of starch (such as swelling capacity, pasting properties, and digestibility) for developing novel low-digestibility starch–protein products. |
| first_indexed | 2024-03-11T05:37:52Z |
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| id | doaj.art-7e26c694effb4a1db69e44a07563faab |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-11T05:37:52Z |
| publishDate | 2023-03-01 |
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| series | Foods |
| spelling | doaj.art-7e26c694effb4a1db69e44a07563faab2023-11-17T16:41:00ZengMDPI AGFoods2304-81582023-03-01127141810.3390/foods12071418The Mechanism Underlying the Amylose-Zein Complexation Process and the Stability of the Molecular Conformation of Amylose-Zein Complexes in Water Based on Molecular Dynamics SimulationChaofan Wang0Na Ji1Lei Dai2Yang Qin3Rui Shi4Liu Xiong5Qingjie Sun6Key Laboratory of Food Processing Technology and Quality Control in Shandong Province, College of Food Science and Engineering, Shandong Agricultural University, Tai’an 271018, ChinaCollege of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, ChinaCollege of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, ChinaCollege of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, ChinaDepartment of Food Science and Technology, College of Light Industry and Food Engineering, Nanjing Forestry University, Nanjing 210037, ChinaCollege of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, ChinaCollege of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, ChinaThe aim of this study was to employ molecular dynamics simulations to elucidate the mechanism involved in amylose–zein complexation and the stability of the molecular conformation of amylose–zein complexes in water at the atomic and molecular levels. The average root mean square deviation and radius of gyration were lower for amylose–zein complexes (1.11 nm and 1 nm, respectively) than for amylose (2.13 nm and 1.2 nm, respectively), suggesting a significantly higher conformational stability for amylose–zein complexes than for amylose in water. The results of radial distribution function, solvent-accessible surface area, and intramolecular and intermolecular hydrogen bonds revealed that the amylose–zein interaction inhibited water permeation into the amylose cavity, leading to enhanced conformational stabilities of the V-type helical structure of amylose and the amylose–zein complexes. Furthermore, the amylose in amylose–zein complexes displayed the thermodynamically stable <sup>4</sup>C<sub>1</sub> conformation. These findings can provide theoretical guidance in terms of the application of protein on starch processing aiming to improve the physicochemical and functional properties of starch (such as swelling capacity, pasting properties, and digestibility) for developing novel low-digestibility starch–protein products.https://www.mdpi.com/2304-8158/12/7/1418molecular dynamics simulationamylosezeincomplexationconformational stability |
| spellingShingle | Chaofan Wang Na Ji Lei Dai Yang Qin Rui Shi Liu Xiong Qingjie Sun The Mechanism Underlying the Amylose-Zein Complexation Process and the Stability of the Molecular Conformation of Amylose-Zein Complexes in Water Based on Molecular Dynamics Simulation Foods molecular dynamics simulation amylose zein complexation conformational stability |
| title | The Mechanism Underlying the Amylose-Zein Complexation Process and the Stability of the Molecular Conformation of Amylose-Zein Complexes in Water Based on Molecular Dynamics Simulation |
| title_full | The Mechanism Underlying the Amylose-Zein Complexation Process and the Stability of the Molecular Conformation of Amylose-Zein Complexes in Water Based on Molecular Dynamics Simulation |
| title_fullStr | The Mechanism Underlying the Amylose-Zein Complexation Process and the Stability of the Molecular Conformation of Amylose-Zein Complexes in Water Based on Molecular Dynamics Simulation |
| title_full_unstemmed | The Mechanism Underlying the Amylose-Zein Complexation Process and the Stability of the Molecular Conformation of Amylose-Zein Complexes in Water Based on Molecular Dynamics Simulation |
| title_short | The Mechanism Underlying the Amylose-Zein Complexation Process and the Stability of the Molecular Conformation of Amylose-Zein Complexes in Water Based on Molecular Dynamics Simulation |
| title_sort | mechanism underlying the amylose zein complexation process and the stability of the molecular conformation of amylose zein complexes in water based on molecular dynamics simulation |
| topic | molecular dynamics simulation amylose zein complexation conformational stability |
| url | https://www.mdpi.com/2304-8158/12/7/1418 |
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