Characterization and structural analysis of prophenoloxidase in mud crab Scylla serrata and discovering novel chemical inhibitors through virtual screening

Prophenoloxidase is a metalloprotinase and closely associated with the copper proteins family like hemocyanin; both are extracellular proteins that are structurally similar and functionally vary in their roles. In this study, we used the mud crab Scylla serrata as a model organism to explore the mec...

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Bibliographic Details
Published in:Structural chemistry 2020-08, Vol.31 (4), p.1563-1584
Main Authors: Jeyachandran, Sivakamavalli, Chandrabose, Selvaraj, Singh, Sanjeev Kumar, Baskaralingam, Vaseeharan, Park, Kiyun, Kwak, Ihn-Sil
Format: Article
Language:English
Subjects:
Binding
Chemistry
Chemistry and Materials Science
Computer Applications in Chemistry
Hemocytes
Homology
Inhibitors
Ligands
Microorganisms
Molecular weight distribution
Mud
Original Research
Physical Chemistry
Polypeptides
Proteins
Screening
Scylla
Structural analysis
Theoretical and Computational Chemistry
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Summary:Prophenoloxidase is a metalloprotinase and closely associated with the copper proteins family like hemocyanin; both are extracellular proteins that are structurally similar and functionally vary in their roles. In this study, we used the mud crab Scylla serrata as a model organism to explore the mechanism of phenoloxidase (PO) and structure analysis through in silico approach also attempting to discover the chemical inhibitors for the protein molecule from different databases. We have purified metalloprotein, prophenoloxidase (proPO), exhibits the 76 kDa molecular weight in SDS-PAGE, widely distributed in hemocytes and consisted of 2 homologous polypeptide chains, proPO1 and proPO2. Enhanced PO activity was observed when using microbial pathogen-associated molecular patterns (MAMPs) and metals as an activator. In vitro and in silico approaches were employed to characterize the structural and functional properties of phenoloxidases, and also we used the virtually screened ligands to check the activity of the protein. Through virtual screening method to screen the new ligands to bind with proPO from zinc and binding databases, the binding interactions are also analyzed via docking scores. This present report paves the way to develop the new immunomodulatory ligands targeting toward the prophenoloxidase and also gives new insights about the structure of the protein.
ISSN:1040-0400
1572-9001
DOI:10.1007/s11224-020-01515-x