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List of peptide properties
DFBP ID - DFBPHEBP0007(Heparin-binding peptide)
DFBP ID DFBPHEBP0007
Peptide sequence FACAAWQWRMKKLGA
Type Native peptide
Peptide/Function name Heparin-binding peptide
Function-activity relationship
Main bioactivity Heparin-binding activity
Otheir bioactivity N.D
Calculated physicochemical properties
Three-letter amino acid Phe-Ala-Cys-Ala-Ala-Trp-Gln-Trp-Arg-Met-Lys-Lys-Leu-Gly-Ala
Single-letter amino acid FACAAWQWRMKKLGA
Peptide length 15
Peptide mass
Experimental mass Theoretical mass
N.D 1767.14 Da c
Net charge 0.00 c
Isoelectric point (pI) 10.59 c
IC50 N.D
pIC50 N.D
GRAVY 0.0133 c
Hydrophilic residue ratio 66.67% c
Peptide calculator
To calculate the physicochemical properties of bioactive peptide.
Peptide source & Food-borne protein(s) search
Classification Animal
Organism/Source Bovine milk protein
Precursor protein Lactoferrin-derived peptide
Residue position f(17-31)
Precursor protein(s) search
No matching precursor protein found
Link-research
There are no literature reports on the discovery of this sequence in other food-source proteins.
Biological/Functional activity & target protein
Heparin-binding activity

The peptide 13 showed potent heparin-binding activity, as shown in Table 1.

Table 1. Synthesized peptides and their heparin-binding activities a.
Num.
Peptide sequence
Heparin-binding activity
1
FKCRRWQWRMKKLGA
++
2
FACAAWQWAMAALGA

3
FACAAWQWAMAKLGA
±
4
FACAAWQWAMKALGA±
5
FACAAWQWRMAALGA
6
FACARWQWAMAALGA
7
FACRAWQWAMAALGA
8
FKCAAWQWAMAALGA
9
FKCRRWQWAMAALGA±
10
FACRRWQWAMAALGA±
11
FKCARWQWAMAALGA±
12
FKCRAWQWAMAALGA
13
FACAAWQWRMKKLGA++
14
FACAAWQWAMKKLGA±
15
FACAAWQWRMAKLGA±
16
FACAAWQWRMKALGA±
17
FACRRWQWRMAALGA+
18
FKCAAWQWAMKKLGA+
19
FKCAAWQWRMAALGA
20
FACARWQWAMAKLGA±
21
FACRAWQWAMAKLGA
a Peptide 1 corresponds to a part of the N-terminal region of bovine lactoferrin. Peptide 2-21 are peptides obtained by substituting partial amino acid mutations of peptide 1. The amino acid residues are expressed using the one-letter symbol.
Specific target protein(s) N.D
Taste properties & Structure
Bitterness
Literature report N.D
Bitter prediction tools No prediction can be made about the peptide bitterness. prediction
SMILES N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(C)C)C(=O)NCC(=O)N[C@@]([H])(C)C(=O)O
Preparation method
Mode of preparation

Synthetic peptide

Enzyme(s)/starter culture

Peptides were synthesized from 9-fluorenylmethoxycarbonyl amino acid active esters on a preactivated cellulose membrane using the SPOTsTM system (Genosys Biotechnologies, Inc.).

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

The heparin-binding site of bovine lactoferrin is proposed to be the sequence BXBB at positions 18–21 and 25–28 and BB at 38–39. The heparin-binding peptide that was isolated from bovine lactoferrin altered its conformation upon interaction with heparin.

Database cross-references
BIOPEP-UWM [D1] 3764
APD [D2] -
BioPepDB [D3] -
MBPDB [D4] -
Reference(s)
Primary literature Shimazaki K, Tazume T, Uji K, Tanaka M, Kumura H, Mikawa K, Shimo-Oka T. Properties of a heparin-binding peptide derived from bovine lactoferrin. J Dairy Sci. 1998 Nov;81(11):2841-9.
PMID: 9839225
Other literature(s) N.D
PubDate 1998
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