A biophysical approach of tyrphostin AG879 binding information in: bovine serum albumin, human ErbB2, c-RAF1 kinase, SARS-CoV-2 main protease and angiotensin-converting enzyme 2

Abstract

Viral infections cause significant health problems all over the world, and it is critical to develop treatments for these problems. Antivirals that target viral genome-encoded proteins frequently cause the virus to become more resistant to treatment. Because viruses rely on several cellular proteins and phosphorylation processes that are essential to their life cycle, drugs targeting host-based targets could be a viable treatment option. To reduce costs and improve efficiency, existing kinase inhibitors could be repurposed as antiviral medications; however, this method rarely works, and specific biophysical approaches are required in the field. Because of the widespread use of FDA-approved kinase inhibitors, it is now possible to better understand how host kinases contribute to viral infection. The purpose of this article is to investigate the tyrphostin AG879 (Tyrosine kinase inhibitor) binding information in Bovine Serum Albumin (BSA), human ErbB2 (HER2), C-RAF1 Kinase (c-RAF), SARS-CoV-2 main protease (COVID 19), and Angiotensin-converting enzyme 2 (ACE-2).

Communicated by Ramaswamy H. Sarma

Keywords:

• tyrphostin AG879
• bovine serum albumin
• human ErbB2
• c-RAF1 kinase
• SARS-CoV-2 main protease
• angiotensin-converting enzyme 2

Acknowledgement

The authors thank VIT for providing ‘VIT RGEMS SEED GRANT’ for carrying out this research work.

Disclosure statement

No potential conflict of interest was reported by the authors.

Additional information

Funding

S.C. was supported by a Grant-in-Aid for Early-Career Scientists fund (KAKENHI No.22K15249) by Japan Society for the Promotion of Science.