BIOPEP-UWM: Peptide Data
ID
Name
Sequence
IY
Chemical Mass
Number of residues
Monoisotopic Mass
EC50
IC50
µM
Additional Information
BIOPEP-UWM database of bioactive peptides SMILES: N[C@H](C(=O)N[C@H](C(=O)O)Cc1ccc(cc1)O)[C@H](CC)C InChI=1S/C15H22N2O4/c1-3-9(2)13(16)14(19)17-12(15(20)21)8-10-4-6-11(18)7-5-10/h4-7,9,12-13,18H,3,8,16H2,1-2H3,(H,17,19)(H,20,21)/t9-,12-,13-/m0/s1 InChIKey: MUFXDFWAJSPHIQ-XDTLVQLUSA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/); ID: M02-001 IC50(EC50) of peptide ranges from 2,1 to 3,7 uM. Loponen J., 2004, Angiotensin converting enzyme inhibitory peptides in Finnish cereals: a database survey. Agric. Food Sci., 13, 39-45 Peptide obtained from the following resources: soybean protein hydrolysate Beermann C., Euler M., Herzberg J., Stahl B., 2009, Anti-oxidative capacity of enzymatically released peptides from soybean protein isolate. Eur. Food Res. Technol., 229, 637–644 amaranth proteins: Barba de la Rosa A. P., Barba Montoya A., Martínez-Cuevas P., Hernández-Ledesma B., León-Galván M. F., De León-Rodríguez A., González C., 2010, Tryptic amaranth glutelin digests induce endothelial nitric oxide production through inhibition of ACE: antihypertensive role of amaranth peptides. Nitric Oxide, 23, 106-111 bovine collagen hydrolysate: Herregods G., Van Camp J., Morel N., Ghesquière B., Gevaert K., Vercruysse L., Dierckx S., Quanten E., Smagghe G., 2011, Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides. J. Agric. Food Chem., 59, 552-558 Antioxidative peptide according to the BIOPEP-UWM database of bioactive peptides (ID 7873); the PlantPepDB database
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