Peptide Database

Peptide NameC8- N27

Function Ontology

Antimicrobial

Antiviral

Antiviral ▸ Anti-HIV ▸ Anti-HIV-1

Antiviral ▸ Antiviral mechanism ▸ Viral fusion inhibition

Antiviral ▸ Antiviral mechanism ▸ Viral fusion inhibition ▸ Fusion inhibitor

Standard StatusStandard

Sequence Length27 amino acids

Chemical FormulaC136H235N45O40

DescriptionStandard

        RQLLSGIVQQQNNLLRAIEAQQHLLQK
    

Molecular Weight3140.60 Da

Isoelectric Point (pI)10.84

Net Charge (pH 7.0)1.85

Net Charge (pH 7.4) 1.59

Charge Density (pH 7.0) 0.0685

GRAVY Index-0.47

Hydrophobic Moment 0.57

Boman Index-0.13

Instability Index67.36

Aliphatic Index 133.70

Aromaticity 0.0000

Extinction Coeff. Reduced 0.00

Extinction Coeff. Oxidized 0.00

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

Amino Acid Composition

TPSA 1443.76

LogP -15.21

H-bond Donors 47.0

H-bond Acceptors 43.0

Rotatable Bonds 113.0

Heavy Atoms 221.0

Ring Count 1.0

Amide Bonds 35.0

3D PDB MODEL

Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber in the current view mode. Use the buttons to zoom.

2D CHEMICAL STRUCTURE

Drag to move

Drag to move. Use the buttons to zoom.

RECORD: Rec_0385419 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

N-TermC12(dodecanoic acid)

C-TermNone

Bio-Activity Profile

Function

Antimicrobial Antiviral

Targetinhibition of peptide against virus-cell fusion on CD4-expressing cells

Activity0.182±0.015 μM

MethodIC50

RECORD: Rec_0417344 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilySynthetic peptide

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

N-TermC12(dodecanoic acid)

C-TermNone

Other ModsC12(dodecanoic acid)

Bio-Activity Profile

Function

Antiviral Fusion inhibition

Targetinhibition of peptide against virus-cell fusion on CD4-expressing cells

Activity0.182±0.015 μM

MethodIC50

Half-LifeMammalian: 1 h; Yeast: 2 min; E. coli: 2 min

PaperVirus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain. | Wexler-Cohen Y, Ashkenazi A, Viard M, Blumenthal R, Shai Y. | FASEB J. 2010 Nov;24(11):4196-202. | DOI:10.1096/fj.09-151704 | PMID:20605950 PMID20605950 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20605950/

RECORD: Rec_0426603 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilySynthetic peptide

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

N-TermC16(hexadecanoic acid)

C-TermNone

Other ModsC16(hexadecanoic acid)

Bio-Activity Profile

Function

Antiviral Anti-HIV-1 Fusion inhibition

TargetHIV-1 | against cell; -cell; HXBc2 cells

Activity0.148±0.004 μM

MethodIC50

Half-LifeMammalian: 1 h; Yeast: 2 min; E. coli: 2 min

PaperVirus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain. | Wexler-Cohen Y, Ashkenazi A, Viard M, Blumenthal R, Shai Y. | FASEB J. 2010 Nov;24(11):4196-202. | DOI:10.1096/fj.09-151704 | PMID:20605950 PMID20605950 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20605950/

FIRST PREV 1 2 3 4

Showing 3 records on this page Ã‚Â· Page 4 of 4