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List of peptide properties
DFBP ID - DFBPOPIO0070(Opioid peptide)
DFBP ID DFBPOPIO0070
Peptide sequence GICACRRRFCPNSERFSGYCRVNGARYVRCCSRR
Type Native peptide
Peptide/Function name Opioid peptide, Corticostatin (CSI)
Function-activity relationship
Main bioactivity Opioid activity
Otheir bioactivity Antimicrobial activity [D1], Multifunctional activity [D2]
Calculated physicochemical properties
Three-letter amino acid Gly-Ile-Cys-Ala-Cys-Arg-Arg-Arg-Phe-Cys-Pro-Asn-Ser-Glu-Arg-Phe-Ser-Gly-Tyr-Cys-Arg-Val-Asn-Gly-Ala-Arg-Tyr-Val-Arg-Cys-Cys-Ser-Arg-Arg
Single-letter amino acid GICACRRRFCPNSERFSGYCRVNGARYVRCCSRR
Peptide length 34
Peptide mass
Experimental mass Theoretical mass
N.D 4003.65 Da c
Net charge 0.00 c
Isoelectric point (pI) 10.25 c
IC50 N.D
pIC50 N.D
GRAVY -0.6382 c
Hydrophilic residue ratio 32.35% c
Peptide calculator
To calculate the physicochemical properties of bioactive peptide.
Peptide source & Food-borne protein(s) search
Classification Animal
Organism/Source Rabbit
Precursor protein Adult rabbit lung
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
Opioid activity

Corticostatin showed opioid activity (data not shown).

Specific target protein(s) N.D
Taste properties & Structure
Bitterness
Literature report N.D
Bitter prediction tools Non-bitter taste prediction
SMILES NCC(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CS)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CO)C(=O)NCC(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(=O)N)C(=O)NCC(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O
Preparation method
Mode of preparation

Extracting 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
Additional information

Corticostatin have previously been isolated from rabbit peritoneal neutrophils and alveolar macrophages and found to be antiviral and antimicrobial agents [1].

Database cross-references
DFBP
[D1] DFBPAMIC0054
[D2] DFBPMUFU0700
BIOPEP-UWM [D3] 2765, 3198
APD [D4] -
BioPepDB [D5] -
MBPDB [D6] -
Reference(s)
Primary literature Zhu QZ, Hu J, Mulay S, Esch F, Shimasaki S, Solomon S. Isolation and structure of corticostatin peptides from rabbit fetal and adult lung. Proc Natl Acad Sci U S A. 1988 Jan;85(2):592-6.
PMID: 2829194
Other literature(s)

[1] Selsted M E, Brown D M, Delange R J, et al. Primary structures of six antimicrobial peptides of rabbit peritoneal neutrophils.[J]. Journal of Biological Chemistry, 1985, 260(8):4579-84.

PubDate 1988
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