Discovery of an Unexplored Protein Structural Scaffold of Serine Protease from Big Blue Octopus (Octopus cyanea): A New Prospective Lead Molecule

Title:Discovery of an Unexplored Protein Structural Scaffold of Serine Protease from Big Blue Octopus (Octopus cyanea): A New Prospective Lead Molecule

Volume: 14 Issue: 2

Author(s): Subhamay Panda*Leena Kumari

Affiliation:

• Department of Pharmacy, Gupta College of Technological Sciences, Ashram More, Asansol- 713301,India

Keywords: Serine protease, big blue octopus, Octopus cyanea, molecular model, drug designing, natural lead molecule.

Abstract: Background: Serine proteases are a group of enzymes that hydrolyses the peptide bonds in proteins. In mammals, these enzymes help in the regulation of several major physiological functions such as digestion, blood clotting, responses of immune system, reproductive functions and the complement system.

Objective: Serine proteases obtained from the venom of Octopodidae family is a relatively unexplored area of research. In the present work, we tried to effectively utilize comparative composite molecular modeling technique. Our key aim was to propose the first molecular model structure of unexplored serine protease 5 derived from big blue octopus. The other objective of this study was to analyze the distribution of negatively and positively charged amino acid over molecular modeled structure, distribution of secondary structural elements, hydrophobicity molecular surface analysis and electrostatic potential analysis with the aid of different bioinformatic tools.

Methods: In the present study, molecular model has been generated with the help of I-TASSER suite. Afterwards the refined structural model was validated with standard methods. For functional annotation of protein molecule we used Protein Information Resource (PIR) database. Serine protease 5 of big blue octopus was analyzed with different bioinformatical algorithms for the distribution of negatively and positively charged amino acid over molecular modeled structure, distribution of secondary structural elements, hydrophobicity molecular surface analysis and electrostatic potential analysis. The functionally critical amino acids and ligand- binding site (LBS) of the proteins (modeled) were determined using the COACH program.

Result: The molecular model data in cooperation to other pertinent post model analysis data put forward molecular insight to proteolytic activity of serine protease 5, which helps in the clear understanding of procoagulant and anticoagulant characteristics of this natural lead molecule.

Conclusion: Our approach was to investigate the octopus venom protein as a whole or a part of their structure that may result in the development of new lead molecule.

Cite this article as:

Panda Subhamay*, Kumari Leena, Discovery of an Unexplored Protein Structural Scaffold of Serine Protease from Big Blue Octopus (Octopus cyanea): A New Prospective Lead Molecule, Current Drug Discovery Technologies 2017; 14 (2) . https://dx.doi.org/10.2174/1570163814666170102141931

DOI https://dx.doi.org/10.2174/1570163814666170102141931	Print ISSN 1570-1638
Publisher Name Bentham Science Publisher	Online ISSN 1875-6220