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Interaction between β-lactoglobulin and EGCG under high-pressure by molecular dynamics simulation

The binding between β-lactoglobulin and epigallocatechin gallate (EGCG) under the pressure of 600 MPa was explored using molecular docking and molecular dynamics (MD) simulation. EGCG bound mainly in two regions with site 1 in internal cavity of the β-barrel and site 2 on the surface of protein. 150...

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Detalles Bibliográficos
Autores principales: Huang, Yechuan, Zhang, Xicai, Suo, Huayi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8691620/
https://www.ncbi.nlm.nih.gov/pubmed/34932559
http://dx.doi.org/10.1371/journal.pone.0255866
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author Huang, Yechuan
Zhang, Xicai
Suo, Huayi
author_facet Huang, Yechuan
Zhang, Xicai
Suo, Huayi
author_sort Huang, Yechuan
collection PubMed
description The binding between β-lactoglobulin and epigallocatechin gallate (EGCG) under the pressure of 600 MPa was explored using molecular docking and molecular dynamics (MD) simulation. EGCG bound mainly in two regions with site 1 in internal cavity of the β-barrel and site 2 on the surface of protein. 150 ns MD was performed starting from the structure with the optimal binding energy at the two sites in molecular docking, respectively. It was found that the protein fluctuated greatly when small molecule bound to site 2 at 0.1 MPa, and the protein fluctuation and solvent accessible surface area became smaller under high-pressure. The binding of small molecules made the protein structure more stable with increasing of α-helix and β-sheet, while high-pressure destroyed α-helix of protein. The binding energy of small molecules at site 1was stronger than that at site 2 under 0.1 MPa, with stronger van der Waals and hydrophobic interaction at site 1 while more hydrogen bonds were present at site 2. The binding energy of both sites weakened under high-pressure, especially at site 1, causing the binding force to be weaker at site 1 than that at site 2 under high-pressure.
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spelling pubmed-86916202021-12-22 Interaction between β-lactoglobulin and EGCG under high-pressure by molecular dynamics simulation Huang, Yechuan Zhang, Xicai Suo, Huayi PLoS One Research Article The binding between β-lactoglobulin and epigallocatechin gallate (EGCG) under the pressure of 600 MPa was explored using molecular docking and molecular dynamics (MD) simulation. EGCG bound mainly in two regions with site 1 in internal cavity of the β-barrel and site 2 on the surface of protein. 150 ns MD was performed starting from the structure with the optimal binding energy at the two sites in molecular docking, respectively. It was found that the protein fluctuated greatly when small molecule bound to site 2 at 0.1 MPa, and the protein fluctuation and solvent accessible surface area became smaller under high-pressure. The binding of small molecules made the protein structure more stable with increasing of α-helix and β-sheet, while high-pressure destroyed α-helix of protein. The binding energy of small molecules at site 1was stronger than that at site 2 under 0.1 MPa, with stronger van der Waals and hydrophobic interaction at site 1 while more hydrogen bonds were present at site 2. The binding energy of both sites weakened under high-pressure, especially at site 1, causing the binding force to be weaker at site 1 than that at site 2 under high-pressure. Public Library of Science 2021-12-21 /pmc/articles/PMC8691620/ /pubmed/34932559 http://dx.doi.org/10.1371/journal.pone.0255866 Text en © 2021 Huang et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Huang, Yechuan
Zhang, Xicai
Suo, Huayi
Interaction between β-lactoglobulin and EGCG under high-pressure by molecular dynamics simulation
title Interaction between β-lactoglobulin and EGCG under high-pressure by molecular dynamics simulation
title_full Interaction between β-lactoglobulin and EGCG under high-pressure by molecular dynamics simulation
title_fullStr Interaction between β-lactoglobulin and EGCG under high-pressure by molecular dynamics simulation
title_full_unstemmed Interaction between β-lactoglobulin and EGCG under high-pressure by molecular dynamics simulation
title_short Interaction between β-lactoglobulin and EGCG under high-pressure by molecular dynamics simulation
title_sort interaction between β-lactoglobulin and egcg under high-pressure by molecular dynamics simulation
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8691620/
https://www.ncbi.nlm.nih.gov/pubmed/34932559
http://dx.doi.org/10.1371/journal.pone.0255866
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