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Study of molecular surface property of phospholipase a2 (pla2) from Naja naja

Author(s): Gomase VS | Gangawane AK | More AR

Journal: International Journal of Chemical Research
ISSN 0975-3699

Volume: 1;
Issue: 1;
Start page: 01;
Date: 2009;
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Keywords: phospholipases a2 | epitope | hydrophobicity | MHC | surface activity | SVM | PSSM | peptide vaccine

This study was designed to elucidate the signalling pathways by which secretary phospholipasea2 (sPLA2s) induce in vitro neutrophil migration and PLA2 inhibits platelet aggregation in PRP and explainsthe decreased clot retraction and retarded and compromised elasticity build up. Naja naja venoms arecomplex and contain several toxic components, including neurotoxins and phospholipases A2 that causepost-synaptic neuromuscular blockade with respiratory paralysis and cardiac arrest. The antigenic epitopeson phospholipase a2 (Pla2) are important determinant of protection against venom. In this analysis, wefound the antigenic epitopes 29-GRGGSGTPVDD-39, 77-TCKGDNNACA-86, of protein called the antigenicdeterminant or the epitope is sufficient for eliciting the desired immune response. Also predict the MHCbinder and these MHC Class peptide segments are from a set of aligned peptides known to bind to a givenmajor histocompatibility complex (MHC) molecule as the predictor of MHC-peptide binding. Binding abilityprediction of antigen peptides to MHC class molecules is important in vaccine development. The methodintegrates prediction of peptide MHC class binding; proteasomal C terminal cleavage efficiency of protein.

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