Peptide Database

Peptide NameEsculentin-2P (Frogs, amphibians, animals)

Function Ontology

Antimicrobial

Antiviral

Antiviral ▸ Antiviral mechanism ▸ Viral entry inhibition

Membrane / Ion-channel modulation ▸ Sodium channel modulation ▸ Sodium channel inhibitor cross

Standard StatusStandard

Sequence Length37 amino acids

Chemical FormulaC176H296N50O45S2

DescriptionStandard

        GFLSIFRGVAKFASKGLGKDLARLGVNLVACKISKQC
    

Molecular Weight3896.67 Da

Isoelectric Point (pI)10.21

Net Charge (pH 7.0)5.74

Net Charge (pH 7.4) 5.50

Charge Density (pH 7.0) 0.1550

GRAVY Index0.48

Hydrophobic Moment 0.75

Boman Index0.13

Instability Index16.78

Aliphatic Index 108.11

Aromaticity 0.0811

Extinction Coeff. Reduced 0.00

Extinction Coeff. Oxidized 125.00

The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.

Amino Acid Composition

TPSA 1548.99

LogP -14.27

H-bond Donors 57.0

H-bond Acceptors 53.0

Rotatable Bonds 136.0

Heavy Atoms 273.0

Ring Count 3.0

Amide Bonds 38.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0010511 VERIFIED: YES

Provenance & Taxonomy

OrganismLithobates pipiens [Animal]

FamilyRanatuerin

Tax ID8404

Structure & Mods

Configdisulfide-constrained cyclic peptide [Cyclic]

Chiralitycanonical L-amino-acid peptide [L]

N-TermNone

C-TermCyclization of a C-terminal Cys residue (forming a disulfide bond)

Disulfide31-37

Other ModsThere is a disulfide bond between Cys31 and Cys37.; Cyclization of a C-terminal Cys residue (forming a disulfide bond)

Bio-Activity Profile

Function

Antiviral Anti-FV3 Entry inhibition

TargetFrog Virus 3

Activity500 μM

Method% inhibition

Half-LifeMammalian: 30 h; Yeast: >20 h; E. coli: >10 h

PaperInactivation of frog virus 3 and channel catfish virus by esculentin-2P and ranatuerin-2P, two antimicrobial peptides isolated from frog skin. | Chinchar VG, Wang J, Murti G, Carey C, Rollins-Smith L. | Virology. 2001 Sep 30;288(2):351-7. | DOI:10.1006/viro.2001.1080 | PMID:11601906 PMID11601906 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/11601906/

RECORD: Rec_0015734 VERIFIED: YES

Provenance & Taxonomy

OrganismRana pipiens [Animal]

FamilyEsculentin

Structure & Mods

Configside-chain cyclized peptide [Cyclic]

Chiralitycanonical L-amino-acid peptide [L]

N-TermNone

C-TermCyclization

Disulfide31-37

Bio-Activity Profile

Function

Antimicrobial Antiviral

TargetChannel Catfish virus(CCV)

RECORD: Rec_0055948 VERIFIED: YES

Provenance & Taxonomy

OrganismRana pipiens [Animal]

FamilyEsculentin

Structure & Mods

Configside-chain cyclized peptide [Cyclic]

Chiralitycanonical L-amino-acid peptide [L]

N-TermNone

C-TermCyclization

Disulfide31-37

Bio-Activity Profile

Function

Antimicrobial Antiviral

RECORD: Rec_0056154 VERIFIED: YES

Provenance & Taxonomy

OrganismLithobates pipiens [Animal]

FamilyRanatuerin

Tax ID8404

Structure & Mods

Configdisulfide-constrained cyclic peptide [Cyclic]

Chiralitycanonical L-amino-acid peptide [L]

N-TermNone

C-TermCyclization of a C-terminal Cys residue (forming a disulfide bond)

Disulfide31-37

Other ModsThere is a disulfide bond between Cys31 and Cys37.; Cyclization of a C-terminal Cys residue (forming a disulfide bond)

Bio-Activity Profile

Function

Antiviral Anti-CCV Entry inhibition

TargetChannel Catfish virus (CCV)

Activity50 μM

Method% inhibition

Half-LifeMammalian: 30 h; Yeast: >20 h; E. coli: >10 h

PaperInactivation of frog virus 3 and channel catfish virus by esculentin-2P and ranatuerin-2P, two antimicrobial peptides isolated from frog skin. | Chinchar VG, Wang J, Murti G, Carey C, Rollins-Smith L. | Virology. 2001 Sep 30;288(2):351-7. | DOI:10.1006/viro.2001.1080 | PMID:11601906 PMID11601906 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/11601906/

RECORD: Rec_0143111 VERIFIED: YES

Provenance & Taxonomy

OrganismLithobates pipiens [Animal]

FamilyRanatuerin

Tax ID8404

Structure & Mods

Configdisulfide-constrained cyclic peptide [Cyclic]

Chiralitycanonical L-amino-acid peptide [L]

N-TermNone

C-TermCyclization of a C-terminal Cys residue (forming a disulfide bond)

Disulfide31-37

Other ModsThere is a disulfide bond between Cys31 and Cys37.; Cyclization of a C-terminal Cys residue (forming a disulfide bond)

Bio-Activity Profile

Function

Antiviral Anti-CCV Entry inhibition

TargetFV3,CCV

Half-LifeMammalian: 30 h; Yeast: >20 h; E. coli: >10 h

PaperInactivation of frog virus 3 and channel catfish virus by esculentin-2P and ranatuerin-2P, two antimicrobial peptides isolated from frog skin. | Chinchar VG, Wang J, Murti G, Carey C, Rollins-Smith L. | Virology. 2001 Sep 30;288(2):351-7. | DOI:10.1006/viro.2001.1080 | PMID:11601906 PMID11601906 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/11601906/

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