Peptide properties

1Top 2Function-activity relationship 3Calculated physicochemical properties 4Peptide source & Food-borne protein(s) search 5Biological/Functional activity & target protein 6Taste properties & Structure 7Preparation method 8Stability & Cytotoxicity 9Additional information 10Database cross-references 11Reference(s)

List of peptide properties

DFBP ID - DFBPACEI2048(ACE-inhibitory peptide)

DFBP ID	DFBPACEI2048
Peptide sequence	PNVA
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Pro-Asn-Val-Ala

Single-letter amino acid

PNVA

Peptide length

Peptide mass

Experimental mass	Theoretical mass
399.45 Da	399.44 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.97 ^c

IC₅₀

8.18 ± 0.24 μM

pIC₅₀

-0.913

GRAVY

0.2250^c

Hydrophilic residue ratio

75%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Marine
Organism/Source	Sea cucumber (Acaudina molpadioidea)
Precursor protein	Sea cucumber protein
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR1386 ---- Plant proteins ---- Transcription factor LATE FLOWERING Source.2: DFBPPR1784 ---- Plant proteins ---- Pentatricopeptide repeat-containing protein OTP51, chloroplastic Source.3: DFBPPR1894 ---- Plant proteins ---- Clathrin heavy chain 1 Source.4: DFBPPR1898 ---- Plant proteins ---- Clathrin heavy chain 2 Source.5: DFBPPR2268 ---- Plant proteins ---- Probable glucomannan 4-beta-mannosyltransferase 7 Source.6: DFBPPR2365 ---- Plant proteins ---- Auxin response factor 5 Source.7: DFBPPR2378 ---- Plant proteins ---- Probable sucrose-phosphate synthase 2 Source.8: DFBPPR2731 ---- Plant proteins ---- Eukaryotic translation initiation factor 4G Source.9: DFBPPR2811 ---- Plant proteins ---- Protein TIFY 6a Source.10: DFBPPR2982 ---- Plant proteins ---- SKP1-like protein 5 Source.11: DFBPPR2993 ---- Plant proteins ---- Beta-glucosidase 5 Source.12: DFBPPR3053 ---- Plant proteins ---- Beta-glucosidase 18 Source.13: DFBPPR3104 ---- Plant proteins ---- Beta-glucosidase 3 Source.14: DFBPPR3307 ---- Plant proteins ---- Endoglucanase 18 Source.15: DFBPPR3571 ---- Plant proteins ---- Probable inorganic phosphate transporter 1-8 Source.16: DFBPPR3809 ---- Plant proteins ---- DEAD-box ATP-dependent RNA helicase 52A Source.17: DFBPPR3818 ---- Plant proteins ---- 26S proteasome regulatory subunit 4 homolog Source.18: DFBPPR3888 ---- Plant proteins ---- Endoglucanase 24 Source.19: DFBPPR3977 ---- Plant proteins ---- Formin-like protein 5 Source.20: DFBPPR4105 ---- Plant proteins ---- Squamosa promoter-binding-like protein 15 Source.21: DFBPPR4705 ---- Plant proteins ---- 40S ribosomal protein S26 Source.22: DFBPPR4744 ---- Plant proteins ---- BURP domain-containing protein 3 Source.23: DFBPPR5311 ---- Plant proteins ---- Nodulin-20 Source.24: DFBPPR5325 ---- Plant proteins ---- Nodulin-C51 Source.25: DFBPPR5332 ---- Plant proteins ---- Nodulin-20a Source.26: DFBPPR5336 ---- Plant proteins ---- Nodulin-26B Source.27: DFBPPR5342 ---- Plant proteins ---- Nodulin-44 Source.28: DFBPPR5356 ---- Plant proteins ---- Nodulin-23 Source.29: DFBPPR5853 ---- Plant proteins ---- Thioredoxin M-type, chloroplastic Source.30: DFBPPR6875 ---- Plant proteins ---- Eukaryotic translation initiation factor 4G Source.31: DFBPPR7512 ---- Plant proteins ---- Malate synthase, glyoxysomal Source.32: DFBPPR16652 ---- Animal proteins ---- Mitochondrial uncoupling protein 2 Source.33: DFBPPR17365 ---- Animal proteins ---- Phospholipase ABHD3 Source.34: DFBPPR18026 ---- Animal proteins ---- Triokinase/FMN cyclase Source.35: DFBPPR18296 ---- Animal proteins ---- Target of rapamycin complex 2 subunit MAPKAP1 Source.36: DFBPPR19442 ---- Animal proteins ---- Eukaryotic translation initiation factor 3 subunit G Source.37: DFBPPR19833 ---- Animal proteins ---- Contactin-1 Source.38: DFBPPR19881 ---- Animal proteins ---- Mitochondrial uncoupling protein 2 Source.39: DFBPPR20315 ---- Animal proteins ---- Probable arginine--tRNA ligase, mitochondrial Source.40: DFBPPR20490 ---- Animal proteins ---- Ornithine aminotransferase, mitochondrial Source.41: DFBPPR20556 ---- Animal proteins ---- Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1 Source.42: DFBPPR20605 ---- Animal proteins ---- 26S proteasome non-ATPase regulatory subunit 13 Source.43: DFBPPR21096 ---- Animal proteins ---- Kinesin light chain 4 Source.44: DFBPPR21378 ---- Animal proteins ---- Kinesin light chain 3 Source.45: DFBPPR21506 ---- Animal proteins ---- Origin recognition complex subunit 3 Source.46: DFBPPR21602 ---- Animal proteins ---- Aspartate beta-hydroxylase domain-containing protein 1 Source.47: DFBPPR21873 ---- Animal proteins ---- Vitrin Source.48: DFBPPR22182 ---- Animal proteins ---- Protein TOPAZ1 Source.49: DFBPPR8614 ---- Animal proteins ---- Triokinase/FMN cyclase Source.50: DFBPPR8669 ---- Animal proteins ---- Heme oxygenase 1 Source.51: DFBPPR9604 ---- Animal proteins ---- Mitochondrial uncoupling protein 2 Source.52: DFBPPR10168 ---- Animal proteins ---- TALPID3 protein Source.53: DFBPPR10189 ---- Animal proteins ---- Sonic hedgehog protein Source.54: DFBPPR10414 ---- Animal proteins ---- Pre-mRNA-processing factor 19 Source.55: DFBPPR10602 ---- Animal proteins ---- DNA (cytosine-5)-methyltransferase 3A Source.56: DFBPPR10653 ---- Animal proteins ---- Contactin-1 Source.57: DFBPPR10919 ---- Animal proteins ---- Ski oncogene Source.58: DFBPPR11536 ---- Animal proteins ---- Putative Polycomb group protein ASXL2 Source.59: DFBPPR12975 ---- Animal proteins ---- Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1 Source.60: DFBPPR13315 ---- Animal proteins ---- Ski oncogene Source.61: DFBPPR13342 ---- Animal proteins ---- Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1 Source.62: DFBPPR13845 ---- Animal proteins ---- Target of rapamycin complex 2 subunit MAPKAP1 Source.63: DFBPPR13854 ---- Animal proteins ---- Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1 Source.64: DFBPPR13950 ---- Animal proteins ---- Protein TOPAZ1 Source.65: DFBPPR14332 ---- Marine protein ---- Ribulose bisphosphate carboxylase large chain Source.66: DFBPPR14748 ---- Marine protein ---- 4-trimethylaminobutyraldehyde dehydrogenase Source.67: DFBPPR14881 ---- Microorganism protein ---- Decapping and exoribonuclease protein 1 Source.68: DFBPPR15369 ---- Microorganism protein ---- 2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 Source.69: DFBPPR15590 ---- Microorganism protein ---- Protein transport protein SEC9 Source.70: DFBPPR15651 ---- Microorganism protein ---- Altered inheritance of mitochondria protein 34, mitochondrial Source.71: DFBPPR15815 ---- Microorganism protein ---- Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase
Link-research Inductive analysis	There are no literature reports on the discovery of this sequence in other food-source proteins.

Biological/Functional activity & target protein

ACE-inhibitory activity

The peptide PNVA showed potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 8.18 ± 0.24 μM.
Molecular docking showed that PNVA formed a larger number of hydrogen bonds with ACE than NVA, while the proline at the N-terminal of peptide can affect the orientation of the binding site of ACE.
The crystal structures of ACE (PDB ID: 2XYD) bound with peptides were obtained from the Protein Data Bank (http://www.rcsb.org) for the docking studies.

Specific target protein(s)

Specific Target Protein(s):
Angiotensin-converting enzyme

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Non-bitter taste ^prediction

SMILES

N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Trypsin (2.5 kU/g protein) and papain (2.5 kU/g protein) were added to Acaudina molpadioidea body wall protein solution and digested in a 50 ℃ water bath for 4 h.

Stability & Cytotoxicity

Peptide stability

Literature report:	N.D
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

In this study, the researchers demonstrated that the addition of exogenous proline to Acaudina molpadioidea protein hydrolysates through the plastein reaction is a promising method to enhance the activity of natural ACE-inhibitory peptides.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Li J, Liu Z, Zhao Y, Zhu X, Yu R, Dong S, Wu H. Novel Natural Angiotensin Converting Enzyme (ACE)-Inhibitory Peptides Derived from Sea Cucumber-Modified Hydrolysates by Adding Exogenous Proline and a Study of Their Structure⁻Activity Relationship. Mar Drugs. 2018 Aug 4;16(8):271. PMID: 30081563 DOI: 10.3390/md16080271
Other literature(s)	N.D
PubDate	2018