Isolation, Identification and in-Silico Characterization of Bioactive Peptide from the Venom Sac of Conus inscriptus

Vidyalatha Jakkana; Shanti Prabha Yamala

doi:10.52756/ijerr.2024.v38.001

Authors

Vidyalatha Jakkana Department of Biology, Zilla Parishad High School, Vaddadi, Visakhapatnam, Andhra Pradesh, India http://orcid.org/0009-0003-3397-7846
Shanti Prabha Yamala Department of Zoology, Dr. V.S. Krishana Govt. Degree & PG College (Autonomous), Visakhapatnam, Andhra Pradesh, India http://orcid.org/0009-0006-9198-5969

DOI:

https://doi.org/10.52756/ijerr.2024.v38.001

Keywords:

Antioxidant activity, Anti-inflammatory activity, PMF, SOPMA, Phyre2, Conotoxin

Abstract

Nature has been the source of new medications since ancient times, and at least half of all commercialised pharmaceuticals have been made from renewable resources to treat various illnesses, including pain, inflammation, and infection. In recent years, interest has risen in bioprospecting of new bioactive peptides, especially for medical and health-related applications. Therefore, the production of functional meals is starting to get recognition for its potential to enhance quality of life when combined with a healthy lifestyle. In view of this, the current work aimed to isolate, purify, and identify bioactive peptides from Conus inscriptus venom sac protein extracts, with an emphasis on antioxidant and anti-inflammatory properties. The findings reveal that the DPPH radical scavenging activity, albumin denaturation, and HRBC membrane stabilisation inhibition activities of Conus inscriptus venom sac crude protein extracts are 23.76±2.4, 66.23±3.1, and 57.32±2.6% respectively. Secondary screening of purified protein fractions obtained through sephadex G100 gel filtration exhibited increased anti-inflammatory efficacy from fractions 19 to 23. Electrophoresis and PMF analysis revealed that the purified anti-inflammatory peptide was homogenous with a molecular weight of 12 KDa, and it was identified as a conotoxin MI15b precursor. The 3D model of conotoxin exhibits the highest similarity with template c6nk9A with a confidence of 54.1%, and its function was predicted as a potassium ion channel inhibitor. The findings of the Insilco characterisation of the conotoxin MI15b precursor concluded that this protein might serve as an anti-inflammatory agent and may be responsible for therapeutic actions in the medical management of many inflammatory-related disorders.

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