Peptide Database

Peptide NameAngiotensin I converting enzyme inhibitior 11

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 Length5 amino acids

Chemical FormulaC32H46N6O6

DescriptionStandard

        VFKAF
    

Molecular Weight610.74 Da

Isoelectric Point (pI)8.72

Net Charge (pH 7.0)0.73

Net Charge (pH 7.4) 0.52

Charge Density (pH 7.0) 0.1466

GRAVY Index1.54

Hydrophobic Moment 0.80

Boman Index0.52

Instability Index-22.06

Aliphatic Index 78.00

Aromaticity 0.4000

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 205.74

LogP 0.63

H-bond Donors 7.0

H-bond Acceptors 7.0

Rotatable Bonds 18.0

Heavy Atoms 44.0

Ring Count 2.0

Amide Bonds 4.0

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_0017018 VERIFIED: YES

Provenance & Taxonomy

OrganismMactra veneriformis [Animal]

FamilyAngiotensin

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Enzyme inhibitory ACE inhibitory

TargetAngiotensin-converting enzyme

Activity100.1 μM

MethodIC50

RECORD: Rec_0402820 VERIFIED: YES

Provenance & Taxonomy

Organismnot reported [other]

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Antihypertensive ACE inhibitory

TargetAngiotensin-converting enzyme (ACE)

Activity100.1

PaperLiu R., Zhu Y., Chen J., Wu H., Shi L., Wang X., Wang L.. Characterization of ACE inhibitory peptides from Mactra veneriformis hydrolysate by nano-liquid chromatography electrospray ionization mass spectrometry (Nano-LC-ESI-MS) and molecular docking. Mar. Drugs, 12, 3917-3928, 2014. Evidence URLhttps://pmc.ncbi.nlm.nih.gov/articles/PMC4113806/