Peptide Database

Peptide NameUnnamed

Function Ontology

Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive

Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory

Other / Curated residual function label ▸ Generic enzyme inhibition annotation

Standard StatusStandard

Sequence Length6 amino acids

Chemical FormulaC29H56N14O8

DescriptionStandard

        RKRAAQ
    

Molecular Weight728.84 Da

Isoelectric Point (pI)12.00

Net Charge (pH 7.0)2.76

Net Charge (pH 7.4) 2.55

Charge Density (pH 7.0) 0.4598

GRAVY Index-2.13

Hydrophobic Moment 0.34

Boman Index-1.03

Instability Index62.67

Aliphatic Index 33.33

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 401.73

LogP -5.22

H-bond Donors 15.0

H-bond Acceptors 11.0

Rotatable Bonds 26.0

Heavy Atoms 51.0

Ring Count 0.0

Amide Bonds 6.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0147320 VERIFIED: NO

Provenance & Taxonomy

OrganismPhaseolus vulgaris [Plant]

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Enzyme inhibitory ACE inhibitory

TargetACE

RECORD: Rec_0175320 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

TargetAngiotensin-converting enzyme

Activity0.095 μM

MethodIC50

RECORD: Rec_0207092 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/