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MYP_049371
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Basic Information
Unnamed
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Neurological / Signaling ▸ Neuropeptide activity ▸ Neuropeptide
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Standard
4 amino acids
C22H32N4O6
Standard
Sequence
VYAP
Physicochemical Analysis
448.51 Da
5.49
-0.27
-0.48
-0.0668
0.78
0.13
0.52
96.00
97.50
0.2500
1490.00
1490.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
162.06
-0.02
5.0
6.0
9.0
32.0
2.0
3.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0021229 VERIFIED: NO
Provenance & Taxonomy
Sepia officinalis [Animal]
ACE-inhibitory peptide
6610
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
PaperANGIOTENSIN CONVERTING ENZYME INHIBITORY PEPTIDES FROM AQUATIC AND THEIR PROCESSING BY-PRODUCTS: A REVIEW
RECORD: Rec_0033975 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive ACE inhibitory
Angiotensin-converting enzyme (ACE)
6.1
IC50
PaperBalti R., Nedjar-Arroume N., Bougatef A., Guillochon D., Nasri M.. Three novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) using digestive proteases. Food Res. Int., 43, 1136-1143, 2010.
RECORD: Rec_0041787 VERIFIED: YES
Provenance & Taxonomy
Sepia officinalis [Animal]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Neuropeptide Enzyme inhibitory ACE inhibitory
Angiotensin-I converting enzyme
6.1 μM
IC50
RECORD: Rec_0061337 VERIFIED: NO
Provenance & Taxonomy
Sepia officinalis [Animal]
ACE-inhibitory peptide
6610
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
Spontaneously hypertensive rat (SHR)
20.5 mmHg
SBP decrease
PaperIs the structural diversity of tripeptides sufficient for developing functional food additives with satisfactory multiple bioactivities?
RECORD: Rec_0165039 VERIFIED: NO
Provenance & Taxonomy
Actinopterygii [Animal]
7898
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
PaperWhat are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach PMID23871047 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23871047/
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