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List of peptide properties
DFBP ID - DFBPAMIC0084(Antimicrobial peptide)
DFBP ID DFBPAMIC0084
Peptide sequence RIIDLLWRVRRPQKPKFVTVWVR
Type Native peptide
Peptide/Function name Antimicrobial peptide, PMAP-23
Function-activity relationship
Main bioactivity Antimicrobial activity
Otheir bioactivity Anticancer activity [D1]
Calculated physicochemical properties
Three-letter amino acid Arg-Ile-Ile-Asp-Leu-Leu-Trp-Arg-Val-Arg-Arg-Pro-Gln-Lys-Pro-Lys-Phe-Val-Thr-Val-Trp-Val-Arg
Single-letter amino acid RIIDLLWRVRRPQKPKFVTVWVR
Peptide length 23
Peptide mass
Experimental mass Theoretical mass
2962.50 Da 2962.60 Da c
Net charge +6
Isoelectric point (pI) 12.68 c
IC50 N.D
pIC50 N.D
GRAVY -0.2957 c
Hydrophilic residue ratio 56.52% c
Peptide calculator
To calculate the physicochemical properties of bioactive peptide.
Peptide source & Food-borne protein(s) search
Classification Animal
Organism/Source Pig (Sus scrofa)
Precursor protein Myeloid cells
Residue position N.D
Precursor protein(s) search
Link-research
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-, antifungal;
(2) Active against E. coli ML35, E. coli ATCC 25922, S. typhimurium ATCC 14028, P. aeruginosa ATCC 27853 (MIC 16 uM), B. megaterium (local isolate), and S. aureus ATCC 25923 (MIC 2-8 uM, except for P. aeruginosa), as shown in table 1:

Table 1 Antibacterial activity of PMAP-23
Organism and strain
MIC (uM)
E. coli ML35
2
E. coli ATCC 25922
4
S. typhimurium ATCC 14028
8
P. aeruginosa ATCC 27853
16
B. megaterium (local isolate)
2
S. aureus ATCC 25923
4

(3) Also antifungal against C. albicans,  S. cerevisiae and T. beigelii (MIC 2-5 uM) [1].

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])([C@]([H])(CC)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(C(C)C)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])(CCC(=O)N)C(=O)N[C@@]([H])(CCCCN)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O
Preparation method
Mode of preparation Extract without enzyme
Enzyme(s)/starter culture

No enzyme, total RNA was extracted from pig bone marrow cells with guanidinium thiocyanate.

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
Additional information N.D
Database cross-references
DFBP
[D1] DFBPANCA0867
BIOPEP-UWM [D2] -
APD [D3] -
BioPepDB [D4] -
MBPDB [D5] -
Reference(s)
Primary literature Zanetti M, Storici P, Tossi A, Scocchi M, Gennaro R. Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells. J Biol Chem. 1994 Mar 18;269(11):7855-8.
PMID: 8132502
Other literature(s) [1] Lee D G, Kim D H, Park Y, et al. Fungicidal effect of antimicrobial peptide, PMAP-23, isolated from porcine myeloid against Candida albicans[J]. Biochemical & Biophysical Research Communications, 2001, 282(2):570-4.
[2] Gennaro R, Skerlavaj B, Romeo D. Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils[J]. Infection & Immunity, 1989, 57(10):3142.
PubDate 1994
Copyright © 2020. Record / license number: Chongqing ICP No. 2000214