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Lau et al. BMC Complementary and Option Medicine 2013, 13:313 http:biomedcentral1472-688213RESEARCH ARTICLEOpen AccessNovel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MSMSChing Ching Lau1, Noorlidah Abdullah1 and Adawiyah Suriza Shuib1,AbstractBackground: Angiotensin I-converting enzyme (ACE) inhibitors have been reported to reduce mortality in sufferers with hypertension. In comparison to chemosynthetic drugs, ACE inhibitors derived from organic sources for instance food proteins are believed to become safer for consumption and to have fewer adverse effects. Some edible mushrooms have already been reported to drastically minimize blood pressure following oral administration. In addition, mushrooms are recognized to be wealthy in protein content. This tends to make them a possible source of ACE inhibitory peptides. Therefore, the objective of the present study was to isolate and characterise ACE inhibitory peptides from an edible mushroom, Pleurotus cystidiosus. Procedures: ACE inhibitory proteins had been isolated from P. cystidiosus depending on the bioassay guided purification steps, i.e. ammonium sulphate precipitation, reverse phase high efficiency Kinesin-14 site liquid chromatography and size exclusion chromatography. Active fraction was then analysed by LC-MSMS and possible ACE inhibitory peptides identified were chemically synthesized. Impact of in vitro gastrointestinal digestions around the ACE inhibitory activity of your peptides and their inhibition patterns have been evaluated. Outcomes: Two possible ACE inhibitory peptides, AHEPVK and GPSMR had been identified from P. cystidiosus with molecular masses of 679.53 and 546.36 Da, respectively. Both peptides exhibited potentially higher ACE inhibitory activity with IC50 values of 62.8 and 277.5 M, respectively. SEC chromatograms and BIOPEP analysis of those peptides revealed that the peptide sequence of the hexapeptide, AHEPVK, was stable throughout gastrointestinal digestion. The pentapeptide, GPSMR, was hydrolysed right after digestion and it was predicted to release a dipeptide ACE inhibitor, GP, from its precursor. The Lineweaver-Burk plot of AHEPVK showed that this potent and steady ACE inhibitor features a competitive inhibitory impact against ACE. Conclusion: The present study indicated that the peptides from P. cystidiosus could be potential ACE inhibitors. Despite the fact that these peptides had reduce ACE inhibitor.