No abstract

Recent studies manifest an increase of inflammatory diseases at an alarming rate due to gut microbiota dysbiosis, genetic and other environmental factors. Lactic acid bacteria (LAB) are known for their antimicrobial properties and their extensive applications in food and pharmaceutical industries. Cyclic peptides are receiving increased attention due to their remarkable stability to withstand variations in temperature and pH. LAB produces anti-inflammatory that can inhibit lipopolysaccharide-induced production of proinflammatory cytokines in macrophages. The structural backbones of cyclic peptides offer a promising approach for the treatment of chronic inflammatory conditions. The current review aims to present the overview of anti-inflammatory and wound healing properties of LAB-derived cyclic peptides.

A 35 KDa protein referred to as F3 was purified from the seeds of Borreria hispida by precipitation with 80% ammonium sulphate and gel filtration on Sephadex G-100 column. RP-HPLC analysis of protein fraction (F3) on an analytical C-18 column produced a single peak, detected at 220 nm. F3 showed an apparent molecular weight of 35 KDa by SDS PAGE and MALDI-TOF-MS analyses. Peptide mass fingerprinting analysis of F3 showed the closest homology with the sequence of 1-aminocyclopropane-1-carboxylate deaminase of Pyrococcus horikoshii. The protein (F3) exhibited significant cytotoxic activity against lung (A549) and cervical (HeLa) cancer cells in a dose-dependent manner at concentrations ranging from 10 µg to 1000 µg/mL, as revealed by the MTT assay. Cell cycle analysis revealed the increased growth of sub-G0 population in both cell lines exposed to a concentration of 1000 µg/mL of protein fraction F3 as examined from flow cytometry. This is the first report of a protein from the seeds of Borreria hispida with antiproliferative and apoptotic activity in lung (A549) and cervical (HeLa) cancer cells.

Objective : The aim of this study was to screen the antimicrobial activity of trypsin-digested peptides isolated from the protein extracts of Valeriana hardwickii and Senna obtusifolia. Methods: The proteins were extracted from the leaves of V. hardwickii and S. obtusifolia which were analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The protein extracts were digested using trypsin which was identified using reverse-phase high-performance liquid chromatography analysis. Further, the antimicrobial efficacy of the digested peptides was investigated.Result: Peptide extracts of V. hardwickii exhibited potent antifungal and antibacterial activity at the maximum concentration of 1.5 mg/ml. Similarly, S. obtusifolia exhibited increased antifungal and antibacterial activity at the concentration of 1.44 mg/ml.Conclusion: The trypsinized extracts of V. hardwickii and S. obtusifolia were plated against Bacillus subtilis which is a promising antibacterial agent.