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 - DFBPAMIC0091(Antimicrobial peptide)

DFBP ID	DFBPAMIC0091
Peptide sequence	RRRPRPPYLPRPRPPPFFPPRLPPRIPPGFPPRFPPRFP
Type	Native peptide
Peptide/Function name	Antimicrobial peptide, PR-39

Function-activity relationship

Main bioactivity	Antimicrobial activity
Otheir bioactivity	Anticancer activity ^[D1]

Calculated physicochemical properties

Three-letter amino acid

Arg-Arg-Arg-Pro-Arg-Pro-Pro-Tyr-Leu-Pro-Arg-Pro-Arg-Pro-Pro-Pro-Phe-Phe-Pro-Pro-Arg-Leu-Pro-Pro-Arg-Ile-Pro-Pro-Gly-Phe-Pro-Pro-Arg-Phe-Pro-Pro-Arg-Phe-Pro

Single-letter amino acid

RRRPRPPYLPRPRPPPFFPPRLPPRIPPGFPPRFPPRFP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	4720.61 Da ^c

Net charge

+11

Isoelectric point (pI)

13.11 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.3077^c

Hydrophilic residue ratio

71.79%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Pig, Sus scrofa
Precursor protein	Pig intestine
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR9256 ---- Animal proteins ---- Antibacterial protein PR-39
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

Antimicrobial activity

(1) anti-Gram+ & Gram-, wound healing, Cancer cells;
(2) Active against E. coli K12, B. megoturium (lethal conc 0.3 uM), S. typhimurium, Strep. pyogmes, A. calccouceticus (lethal conc 1-3 uM), and B. subtilis (15 uM).

Table 1 Inhibition zone assay of PR-39 with nine different bacteria.
Organism	Strain	Maximum (mm)	Lethal conc. (uM)
E. coli K12	D21	18.3	0.3
E. coli	Bd2221/75	17.6	0.3
S. typhimurium	LT2	15.2	1
P. vulgaris	Pv11	3.5	300
Ps. aeruginosa	OT97	4.5	200
A. calcoaceticus	Ac11	12.5	3
B. megaterium	Bm11	17.4	0.3
B. subtilis	Bs11	10.3	15
Staph. aureus	Cowan 1	3.7	200
Strep. pyogenes	-	14.9	2

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)NCC(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Extract without enzyme
Enzyme(s)/starter culture	No enzyme

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

N.D

Database cross-references

DFBP

[D1]	DFBPANCA0447

[D2]

[D3]

[D4]

[D5]

Reference(s)

Primary literature	Agerberth B, Lee JY, Bergman T, Carlquist M, Boman HG, Mutt V, Jörnvall H. Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides. Eur J Biochem. 1991 Dec 18;202(3):849-54. PMID: 1765098 DOI: 10.1111/j.1432-1033.1991.tb16442.x
Other literature(s)	[1] Hultmark D, Engström A, Andersson K, et al. Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia[J]. Embo Journal, 1983, 2(4):571.
PubDate	1991