Title

Molecular docking analysis of penta galloyl glucose with the bcl-2 family of anti-apoptotic targets

Authors

Karthick Dharmalingam¹, Velvizhi Dharmalingam², Satheesh Durairaj³, Praveen Sharma¹, Selvaraj Jayaraman⁴ & Sarita Choudhary^1,*

Affiliation

¹Department of Biochemistry, All India Institute of Medical Sciences, Jodhpur, Rajasthan- 342005, India; ²Department of Chemistry, Captain Srinivasa Murthy Central Ayurveda Research institute, CCRAS, Ministry of AYUSH, Government of India, Chennai – 600106; ³Department of chemistry, Siddha Central Research institute, Arumbakkam, Chennai - 600106; ⁴Department of Biochemistry, Saveetha Dental College and Hospitals, Saveetha Institute of Medical and Technical Sciences, Saveetha University, Chennai-600 077, India Corresponding author^*

Email

Dr. Sarita Choudhary: sarita.choudhary82@gmail.com; Karthick Dharmalingam - karthickgeo@gmail.com Velvizhi Dharmalingam - velvizhi727@gmail.com Satheesh Durairaj - adsatheesh@gmail.com Praveen Sharma - praveensharma55@gmail.com Selvara Jayaraman - selvarajj.sdc@saveeth.com Sarita Choudhary - sarita.choudhary82@gmail.com

Article Type

Research Article

Date

Received August 10, 2021; Revised October 12, 2021; Accepted October 12, 2021, Published October 31, 2021

Apoptosis requires cellular proteins from the B-cell lymphoma 2 (BCL-2) family linked to breast cancer. Therefore, it is of interest to document the Molecular docking analysis data of penta galloyl glucose with the bcl-2 family of anti-apoptotic targets (Bcl-2, BCL-XL, Caspase 3, and Caspase 9). Data shows that Pentagalloyl glucose have optimal binding features with Bcl-2, BCL-XL, Caspase 3, and Caspase 9 proteins with binding energy of -8.6,-7,-7.5 and 4.4 kcal/mol respectively for further consideration in this context.

Keywords

Breast cancer, apoptosis, penta galloyl glucose, molecular docking

Citation

Dharmalingam et al. Bioinformation 17(10): 861-865 (2021)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

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.