ISOLATION AND PURIFICATION OF ANTIBIOFILM PEPTIDES FROM TRIDAX PROCUMBENS , A MEDICINAL PLANT

Author(s): Choppavarapu Hari Krishna and Kasturi Kondapalli

Abstract: Small peptides are being used as therapeutics in organ transplants and bacterial infections. The objective of present study was aimed to purify and evaluate antibiofilm activity of peptides from the Tridax procumbens. The aerial parts of plant material (leaf, stems and root) was collected, cleaned, shade dried and powered. The powered samples were extracted separately with acetonitrile and formic acetic acid (50:1). The extracted small peptides were partially purified by DEAE cellulose column and then concentrated by lyophilizer. The lyophilized samples were subjected to HPLC for purification. Crude and purified small peptides were analyzed by SDS-PAGE and molecular weight ascertained. Small peptides were evaluated for its biofilm inhibition of Staphylococcus aureus. The extracted small peptide yield was found to be 2%. The quantitative analysis of crude small peptides and purified was found to be 120 and 43 µg/ml respectively. The molecular weight of purified peptides was calculated and was found 4KDA. Small ppeptides exhibited biofilm inhibition of 88.49±0.65% at 100µg/mL and also showed proteolytic and exopolysaccharides at 100µg/mL against S. aureus. In conclusion, the current study showed T. procumbens is a good source for small peptides, acts as a potent biofilm inhibitor. To the best of our knowledge this is the first report on isolation, purification and evaluation of biofilm inhibition of peptides form T. procumbens.

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