Cargando…

Antiproliferative activity and interaction with proteins of N-cyclohexylacrylamide

N-cyclohexylacrylamıde (NCA), the synthesized compound, was evaluated for their cytotoxic activities against HeLa cancer cell line. Also, the current study has been analyzed by the use of molecular docking as protein-ligand interactions play a vital role in drug design. The docking study of NCA was...

Descripción completa

Detalles Bibliográficos
Autores principales: Çankaya, Nevin, Yalçin, Serap
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9637753/
https://www.ncbi.nlm.nih.gov/pubmed/36353361
http://dx.doi.org/10.1016/j.sjbs.2020.04.030
_version_ 1784825254279905280
author Çankaya, Nevin
Yalçin, Serap
author_facet Çankaya, Nevin
Yalçin, Serap
author_sort Çankaya, Nevin
collection PubMed
description N-cyclohexylacrylamıde (NCA), the synthesized compound, was evaluated for their cytotoxic activities against HeLa cancer cell line. Also, the current study has been analyzed by the use of molecular docking as protein-ligand interactions play a vital role in drug design. The docking study of NCA was performed with BCL-2, BCL-W, MCl-1, AKT, BRAF, CDK2, VEGFR, EGFR PARP1, CDK6 proteins. The 3D structures of proteins were obtained from the protein data bank and 3D structure of NCA compounds using GAUSSIAN. The in silico molecular docking results indicated that NCA compound can inhibit cancer-related proteins and can play a role as potential lead compounds for developing new drugs for cancer therapy with chemical modification.
format Online
Article
Text
id pubmed-9637753
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher Elsevier
record_format MEDLINE/PubMed
spelling pubmed-96377532022-11-08 Antiproliferative activity and interaction with proteins of N-cyclohexylacrylamide Çankaya, Nevin Yalçin, Serap Saudi J Biol Sci Original Article N-cyclohexylacrylamıde (NCA), the synthesized compound, was evaluated for their cytotoxic activities against HeLa cancer cell line. Also, the current study has been analyzed by the use of molecular docking as protein-ligand interactions play a vital role in drug design. The docking study of NCA was performed with BCL-2, BCL-W, MCl-1, AKT, BRAF, CDK2, VEGFR, EGFR PARP1, CDK6 proteins. The 3D structures of proteins were obtained from the protein data bank and 3D structure of NCA compounds using GAUSSIAN. The in silico molecular docking results indicated that NCA compound can inhibit cancer-related proteins and can play a role as potential lead compounds for developing new drugs for cancer therapy with chemical modification. Elsevier 2022-11 2020-04-23 /pmc/articles/PMC9637753/ /pubmed/36353361 http://dx.doi.org/10.1016/j.sjbs.2020.04.030 Text en © 2022 Published by Elsevier B.V. on behalf of King Saud University. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Original Article
Çankaya, Nevin
Yalçin, Serap
Antiproliferative activity and interaction with proteins of N-cyclohexylacrylamide
title Antiproliferative activity and interaction with proteins of N-cyclohexylacrylamide
title_full Antiproliferative activity and interaction with proteins of N-cyclohexylacrylamide
title_fullStr Antiproliferative activity and interaction with proteins of N-cyclohexylacrylamide
title_full_unstemmed Antiproliferative activity and interaction with proteins of N-cyclohexylacrylamide
title_short Antiproliferative activity and interaction with proteins of N-cyclohexylacrylamide
title_sort antiproliferative activity and interaction with proteins of n-cyclohexylacrylamide
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9637753/
https://www.ncbi.nlm.nih.gov/pubmed/36353361
http://dx.doi.org/10.1016/j.sjbs.2020.04.030
work_keys_str_mv AT cankayanevin antiproliferativeactivityandinteractionwithproteinsofncyclohexylacrylamide
AT yalcinserap antiproliferativeactivityandinteractionwithproteinsofncyclohexylacrylamide