Interaction of proteinase inhibitors with phospholipid vesicles is modulated by pH

• Published in: International journal of biological macromolecules 2010-11, Vol.47 (4), p.551-557
• Main Authors: Silva-Lucca, Rosemeire A., Faneca, Henrique M.S., de Lima, Maria C. Pedroso, De Caroli, Fernanda P., Assis, M.L., Sampaio, Misako U., Oliva, Maria Luiza V.
• Format: Article
• Language: English
• Subjects: Animals; Bauhinia; Cattle; Circular Dichroism; Fluoresceins - metabolism; Fluorescence spectroscopy; Humans; Hydrogen-Ion Concentration; Liposome; Peptide Hydrolases - chemistry; Peptide Hydrolases - metabolism; Phospholipid; Phospholipids - metabolism; Plant proteinase inhibitors; Protease Inhibitors - chemistry; Protease Inhibitors - metabolism; Protein Structure, Secondary; Spectrometry, Fluorescence; Sus scrofa; Temperature; Trypsin inhibitor; Unilamellar Liposomes - metabolism
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2010.07.011

rBbKI and rBbCI, plant recombinant inhibitors from Bauhinia bauhinioides, and BpuTI from Bauhinia purpurea seeds distinctly and specifically block proteolytic enzymes. The secondary structures of those inhibitors were compared and their interactions with phospholipid vesicles were evaluated by the release of calcein and by intrinsic fluorescence of tryptophan residues. The results show that rBbKI, rBbCI and BpuTI are able to interact with phospholipd vesicles and induce membrane permeabilization in a concentration- and pH-dependent manner. The leakage was rapid and extensive at pH 4.5, but at physiological pH, no calcein release was observed. These results may suggest that upon inflammation or microorganism invasion accompanied by lowering of pH, appropriate conditions may occur for the inhibitors to interact with cell membrane and act on specific proteolytic enzyme.