LC-MS/MS coupled with QSAR modeling in characterising of angiotensin I-converting enzyme inhibitory peptides from soybean proteins.
The importance of soy products in reducing the risk of cardiovascular disease is well documented. Our previous computation study has indicated the presence of several potent ACE inhibitory peptides within soybean proteins which needs to be identified. The aim of the study was to identify ACE inhibitory peptides from soy proteins using LC-MS/MS coupled with quantitative structure-activity relationship (QSAR) model. Soybean protein hydrolysate digested by thermolysin showed an IC50 value of 53.6 μg/mL, decreased slightly to 51.8 μg/mL after adding pepsin, and increased to 115.6 μg/mL after adding trypsin. A total of 34 peptides were characterised from LC-MS/MS. Five novel tripeptides, IVF, LLF, LNF, LSW and LEF, with predicted IC50 values lower than 10 μM were synthesized and validated. The results showed that soybean is an excellent source of ACE inhibitory peptides.
['Gu|Yuchen|Y|', 'Wu|Jianping|J|']
D000595:Amino Acid Sequence D000806:Angiotensin-Converting Enzyme Inhibitors D006868:Hydrolysis D007700:Kinetics D008969:Molecular Sequence Data D010449:Peptide Mapping D010455:Peptides D007703:Peptidyl-Dipeptidase A D021281:Quantitative Structure-Activity Relationship D030262:Soybean Proteins D013025:Soybeans D053719:Tandem Mass Spectrometry D013820:Thermolysin
QSAR model Soybean ACE inhibitory peptides