Peptide Database

Peptide NameACE inhibitory peptide

Function Ontology

Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive

Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory

Enzyme modulation ▸ Enzyme inhibition ▸ DPP-IV inhibition ▸ DPP-IV inhibitory

Membrane / Ion-channel modulation ▸ Calcium channel modulation ▸ Calcium channel inhibitor

Metabolic ▸ Glucose metabolism ▸ Antidiabetic

Standard StatusStandard

Sequence Length13 amino acids

Chemical FormulaC71H128N20O20S

DescriptionStandard

        LRENNKLMLLELK
    

Molecular Weight1613.96 Da

Isoelectric Point (pI)8.59

Net Charge (pH 7.0)0.76

Net Charge (pH 7.4) 0.55

Charge Density (pH 7.0) 0.0587

GRAVY Index-0.42

Hydrophobic Moment 0.25

Boman Index-0.20

Instability Index29.20

Aliphatic Index 150.00

Aromaticity 0.0000

Extinction Coeff. Reduced 0.00

Extinction Coeff. Oxidized 0.00

The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.

Amino Acid Composition

TPSA 687.24

LogP -3.80

H-bond Donors 23.0

H-bond Acceptors 22.0

Rotatable Bonds 60.0

Heavy Atoms 112.0

Ring Count 0.0

Amide Bonds 14.0

3D PDB MODEL

Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber in the current view mode. Use the buttons to zoom.

2D CHEMICAL STRUCTURE

Drag to move

Drag to move. Use the buttons to zoom.

RECORD: Rec_0044344 VERIFIED: YES

Provenance & Taxonomy

OrganismPhaseolus vulgaris [Plant]

FamilyBioactive peptides

Tax ID3885

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

ACE inhibitory Antihypertensive Antioxidant

TargetAngiotensin-converting enzyme

Activity0.093 μM

MethodIC50

RECORD: Rec_0056284 VERIFIED: YES

Provenance & Taxonomy

OrganismPhaseolus vulgaris [Plant]

Tax ID3885.0

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Antidiabetic DPP-IV inhibitory

TargetDipeptidyl peptidase IV

PaperMojica L., Chen K., de Mejia E.G.. Impact of Commercial Precooking of Common Bean (Phaseolus vulgaris) on the Generation of Peptides, After Pepsin-Pancreatin Hydrolysis, Capable to Inhibit Dipeptidyl Peptidase-IV. Journal of Food Science, 80, 188-198, DOI: 10.1111/1750-3841.12726. PMID25495131 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/25495131/

RECORD: Rec_0209384 VERIFIED: YES

Provenance & Taxonomy

OrganismPhaseolus vulgaris [Plant]

Tax ID3885.0

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Antihypertensive ACE inhibitory

TargetAngiotensin-converting enzyme (ACE)

PaperMojica L., Chen K., de Mejia E.G.. Impact of Commercial Precooking of Common Bean (Phaseolus vulgaris) on the Generation of Peptides, After Pepsin-Pancreatin Hydrolysis, Capable to Inhibit Dipeptidyl Peptidase-IV. Journal of Food Science, 80, 188-198, DOI: 10.1111/1750-3841.12726. PMID25495131 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/25495131/

RECORD: Rec_0386792 VERIFIED: YES

Provenance & Taxonomy

OrganismPhaseolus vulgaris [Plant]

Tax ID3885.0

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Antioxidant

PaperMojica L., Chen K., de Mejia E.G.. Impact of Commercial Precooking of Common Bean (Phaseolus vulgaris) on the Generation of Peptides, After Pepsin-Pancreatin Hydrolysis, Capable to Inhibit Dipeptidyl Peptidase-IV. Journal of Food Science, 80, 188-198, DOI: 10.1111/1750-3841.12726. PMID25495131 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/25495131/