Molecular docking analysis of C-phycocyanin with VEGFR2

C-phycocyanin (C-PC) produced from cyanobacterial species finds application in drug development. Therefore, it is of interest to document the molecular binding features of C-PC with the vascular endothelial growth factor receptor 2 (VEGFR2). C-PC showed H-bond interactions with residues on both side...

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Autores principales: Bannu, Saira M, Lomada, Dakshayani, Varala, Sravani, Reddy, Madhava C
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2020
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8573453/
https://www.ncbi.nlm.nih.gov/pubmed/34803261
http://dx.doi.org/10.6026/97320630016869
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author Bannu, Saira M
Lomada, Dakshayani
Varala, Sravani
Reddy, Madhava C
author_facet Bannu, Saira M
Lomada, Dakshayani
Varala, Sravani
Reddy, Madhava C
author_sort Bannu, Saira M
collection PubMed
description C-phycocyanin (C-PC) produced from cyanobacterial species finds application in drug development. Therefore, it is of interest to document the molecular binding features of C-PC with the vascular endothelial growth factor receptor 2 (VEGFR2). C-PC showed H-bond interactions with residues on both sides of the Deusche Forschugsgemein-Schalt (DFG) loop (Asp1046-Phe1047-Gly1048). A hydrophobic association between the activation loop and the DFG residue (Gly1048) helps to inhibit the activity of VEGFR2 kinases. Thus, C-PC is reported as a potential angiogenesis inhibitor for VEGFR2 in combating cancer.
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spelling pubmed-85734532021-11-18 Molecular docking analysis of C-phycocyanin with VEGFR2 Bannu, Saira M Lomada, Dakshayani Varala, Sravani Reddy, Madhava C Bioinformation Research Article C-phycocyanin (C-PC) produced from cyanobacterial species finds application in drug development. Therefore, it is of interest to document the molecular binding features of C-PC with the vascular endothelial growth factor receptor 2 (VEGFR2). C-PC showed H-bond interactions with residues on both sides of the Deusche Forschugsgemein-Schalt (DFG) loop (Asp1046-Phe1047-Gly1048). A hydrophobic association between the activation loop and the DFG residue (Gly1048) helps to inhibit the activity of VEGFR2 kinases. Thus, C-PC is reported as a potential angiogenesis inhibitor for VEGFR2 in combating cancer. Biomedical Informatics 2020-11-30 /pmc/articles/PMC8573453/ /pubmed/34803261 http://dx.doi.org/10.6026/97320630016869 Text en © 2020 Biomedical Informatics https://creativecommons.org/licenses/by/3.0/This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.
spellingShingle Research Article
Bannu, Saira M
Lomada, Dakshayani
Varala, Sravani
Reddy, Madhava C
Molecular docking analysis of C-phycocyanin with VEGFR2
title Molecular docking analysis of C-phycocyanin with VEGFR2
title_full Molecular docking analysis of C-phycocyanin with VEGFR2
title_fullStr Molecular docking analysis of C-phycocyanin with VEGFR2
title_full_unstemmed Molecular docking analysis of C-phycocyanin with VEGFR2
title_short Molecular docking analysis of C-phycocyanin with VEGFR2
title_sort molecular docking analysis of c-phycocyanin with vegfr2
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8573453/
https://www.ncbi.nlm.nih.gov/pubmed/34803261
http://dx.doi.org/10.6026/97320630016869
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