Peptide Database

Peptide NameWQ-SDLD

Function Ontology

Antimicrobial

Antiviral

Antiviral ▸ Anti-HIV ▸ Anti-HIV-1

Antiviral ▸ Antiviral mechanism ▸ Viral fusion inhibition

Standard StatusStandard

Sequence Length30 amino acids

Chemical FormulaC168H262N42O57

DescriptionStandard

        WEEWDKKIEEYTKKIEELIKKSQNQQSDLD
    

Molecular Weight3782.12 Da

Isoelectric Point (pI)4.73

Net Charge (pH 7.0)-3.22

Net Charge (pH 7.4) -3.45

Charge Density (pH 7.0) -0.1075

GRAVY Index-1.77

Hydrophobic Moment 0.69

Boman Index-0.39

Instability Index77.37

Aliphatic Index 65.00

Aromaticity 0.1000

Extinction Coeff. Reduced 12490.00

Extinction Coeff. Oxidized 12490.00

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

Amino Acid Composition

TPSA 1683.90

LogP -13.49

H-bond Donors 56.0

H-bond Acceptors 54.0

Rotatable Bonds 137.0

Heavy Atoms 267.0

Ring Count 5.0

Amide Bonds 33.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0174218 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Antiviral

TargetHIV-1 IIIB

RECORD: Rec_0327711 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

N-TermNone

C-TermNone

Bio-Activity Profile

Function

Antimicrobial Antiviral

TargetHIV-1 IIIB:inhibition of virus infection in MT-2 cells

Activity0.0441 μM

MethodIC50

RECORD: Rec_0377005 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilyFusion-inhibitory peptide

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

N-TermNone

C-TermNone

Bio-Activity Profile

Function

Antiviral Anti-HIV-1 Fusion inhibition

TargetHIV-1 IIIB | MT-2 cells

Activity0.0441 μM

MethodIC50

Half-LifeMammalian: 2.8 h; Yeast: 3 min; E. coli: 2 min

PaperCreating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors. | Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L. | J Virol. 2016 Dec 16;91(1):e01445-16. | DOI:10.1128/JVI.01445-16 | PMID:27795416 PMID27795416 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/27795416/