Extraction of biologically active protein from ayapana (Ayapana triplinervis Vahl) and evaluation of antimicrobial activity

Peptide therapy is an emerging technology in medicine. Plant-based peptide drug discovery would be an effective and target-specific therapeutic agent which overcomes the traditional drawback. The study aims to explore and characterise the potent protein candidate from fresh leaves of Ayapana triplinervis Vahl, to study the efficiency against various clinical pathogens. The proteins have been extracted, precipitated, and characterised. Three methods have been used to extract proteins, and the EB TA (Extraction buffer - TCA acetone) method favours a good yield of protein. The extracted protein was completely solubilised in Tris-Cl (pH 7.4) buffer than other solubilizing buffers. The molecular weight of the extracted proteins was determined by plotting a graph of log Molecular weight with relative migration distance for standards. The proteins separated were less than 30 kDa by all three methods. The proteins extracted by using the EB-TA method elicited antimicrobial activity against E. coli, Staphylococcus aureus, Streptococcus species and MRSA (Methicillin-Resistant Staphylococcus aureus) strains isolated from clinical wounds. The above results suggest that the protein extract of the fresh leaves of Ayapana triplinerve Vahl has potent antibacterial activity.