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 - DFBPACEI0011(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0011
Peptide sequence	LKPNM
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Antihypertensive activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Leu-Lys-Pro-Asn-Met

Single-letter amino acid

LKPNM

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	601.76 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

10.04 ^c

IC₅₀

2.4 uM, 17 uM ^[1]

pIC₅₀

-0.38, -1.23

GRAVY

-0.6600^c

Hydrophilic residue ratio

60%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal, Marine, Fish
Organism/Source	Bonito
Precursor protein	Bonito protein
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR0846 ---- Plant proteins ---- Catalase isozyme B Source.2: DFBPPR2451 ---- Plant proteins ---- Fructose-bisphosphate aldolase 3, cytoplasmic Source.3: DFBPPR2493 ---- Plant proteins ---- Fructose-bisphosphate aldolase 2, cytoplasmic Source.4: DFBPPR4922 ---- Plant proteins ---- Fructose-bisphosphate aldolase 1, cytoplasmic Source.5: DFBPPR5505 ---- Plant proteins ---- Fructose-bisphosphate aldolase, cytoplasmic isozyme Source.6: DFBPPR6485 ---- Plant proteins ---- Fructose-bisphosphate aldolase, cytoplasmic isozyme 2 Source.7: DFBPPR6486 ---- Plant proteins ---- Fructose-bisphosphate aldolase, cytoplasmic isozyme 1 Source.8: DFBPPR19656 ---- Animal proteins ---- Fructose-bisphosphate aldolase B Source.9: DFBPPR10368 ---- Animal proteins ---- Fructose-bisphosphate aldolase B Source.10: DFBPPR10369 ---- Animal proteins ---- Fructose-bisphosphate aldolase B Source.11: DFBPPR10783 ---- Animal proteins ---- Fructose-bisphosphate aldolase C Source.12: DFBPPR11293 ---- Animal proteins ---- RIMS-binding protein 2 Source.13: DFBPPR12248 ---- Animal proteins ---- Fructose-bisphosphate aldolase A Source.14: DFBPPR12573 ---- Animal proteins ---- Fructose-bisphosphate aldolase B Source.15: DFBPPR13678 ---- Animal proteins ---- Fructose-bisphosphate aldolase B Source.16: DFBPPR14109 ---- Marine protein ---- Fructose-bisphosphate aldolase A
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 exhibited strong Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 2.4 uM (or 17 uM, 10 μg/mL ^[1]).
Specific target protein(s)	Specific Target Protein(s): Angiotensin-converting enzyme

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Bitter taste ^prediction

SMILES

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

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Bonito protein was hydrolyzed with Thermolysin.

Stability & Cytotoxicity

Peptide stability

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

Peptide cytotoxicity

Literature report:	Non-Toxin
Prediction:	ToxinPred

Additional information

LKPNM is the prodrug-type ACE inhibitory peptide. Following hydrolysis of LKPNM into LKP by ACE, an 8-fold augmentation in ACE-inhibitory activity was observed.

Database cross-references

DFBP

[D1]	DFBPANHY0279
[D2]	DFBPMUFU0003

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Fujita, H., Yoshikawa, M. LKPNM: a prodrug-type ACE-inhibitory peptide derived from fish protein. Immunopharmacology. 1999, 44, 123-7. DOI: 10.1016/S0162-3109(99)00118-6
Other literature(s)	[1] Yokoyama K, Chiba H, Yoshikawa M. Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito[J]. Journal of the Agricultural Chemical Society of Japan, 1992, 56(10):1541-1545.
PubDate	1999