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 The synthetic peptide analogue in a concentration of 3,4 mM revealed significant radical scavenging properties of 16,7%. Peptide obtained by hydrolysis of a soybean protein isolate (Danone Research, Friedrichsdorf, Germany) by use of trypsin. Found in hydrolysates of sardine muscle proteins. Matsufuji H., Matsui T., Seki E., Osajima K., Nakashima M., Osajima Y., 1994, Angiotensin I-converting enzyme inhibitory peptides in an alkaline proteinase hydrolysate derived from sardine muscle. Biosci. Biotech. Biochem., 58, 2244-2245 Found in 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 Found in 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 Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: M02-001) according to the AHTPDB database; the Binding DB database; the BIOPEP-UWM database of bioactive peptides (ID 7873); the BRENDA database; the ChEMBL database; the EROP-Moscow database; the PlantPepDB database
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