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 FormulaC31H50N8O8

DescriptionStandard

        LLHSPP
    

Molecular Weight662.78 Da

Isoelectric Point (pI)6.74

Net Charge (pH 7.0)-0.15

Net Charge (pH 7.4) -0.41

Charge Density (pH 7.0) -0.0255

GRAVY Index0.07

Hydrophobic Moment 0.32

Boman Index0.30

Instability Index113.67

Aliphatic Index 130.00

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 240.15

LogP -1.11

H-bond Donors 7.0

H-bond Acceptors 9.0

Rotatable Bonds 16.0

Heavy Atoms 47.0

Ring Count 3.0

Amide Bonds 5.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0162269 VERIFIED: NO

Provenance & Taxonomy

Organismnot reported [other]

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Enzyme inhibitory ACE inhibitory

TargetACE

RECORD: Rec_0397616 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

Activity222.0 μM

MethodIC50

RECORD: Rec_0408866 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)

Activity222.0

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/