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Title

Molecular docking and in vitro analysis of peptides from Stolephorus indicus with ACE2

 

Authors

Usha Rani Keshapaga1, Gulam Mohammed Husain2, Surya Satyanarayana Singh3 & Sandeepta Burgula1*

 

Affiliation

1Department of Microbiology, Osmania University, Hyderabad 500007; 2National Research Institute of Unani Medicine for Skin Disorders, Ministry of AYUSH, Government of India, Hyderabad - 500038; 3Department of Biochemistry, Osmania University, Hyderabad 500007.

 

Email

Usha Rani Keshapaga E-mail: usha1824@gmail.com

Gulam Mohammed Husain E-mail: gmhusain@gmail.com

Surya Satyanarayana Singh E-mail: suryasingh.oubioc@gmail.com

Sandeepta Burgula E-mail: s_burgula@osmania.ac.in

 

Article Type

Research Article

 

Date

Received May 1, 2023; Revised May 31, 2023; Accepted May 31, 2023, Published May 31, 2023

 

Abstract

Peptides from Stolephorus indicus (Anchovies) meat lysate were generated using a Bacillus subtilis cysteine protease. The peptides were generated by enzyme hydrolysis after which the hydrolysate containing peptides were analysed by LC-MS/MS. Computer aided analysis of peptides using CASTp server and GOLD software show four peptides having ACE2 inhibitory activity. Further, peptides 1 (8 amino acids), 2 (8 amino acid), 5 (9 amino acids) and 11 (12 amino acids) showed good docking features for binding to ACE2 enzyme active sites, mainly by hydrogen bonding. Peptide 1 (8 amino acids-octa-peptide) having the highest docking score was tested in vitro for ACE2 binding and showed up to 40 % inhibition of ACE2 activity at a concentration of 10mM. Hence, this octa-peptide has a potential role in applications involving ACE2 inhibition thereby leading to the prevention of binding of spike glycoprotein to ACE2 receptor.

 

Keywords

Peptides, cysteine protease, ACE2, hypertension, anchovies.

 

Citation

Keshapaga et al. Bioinformation 19(5): 531-535 (2023)

 

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.