Peptide Database

Peptide NameVpr 33-47

Function Ontology

Antimicrobial

Antiviral

Antiviral ▸ Anti-HIV ▸ Anti-HIV-1

Antiviral ▸ Antiviral mechanism ▸ Viral replication inhibition

Enzyme modulation ▸ Enzyme inhibition ▸ Integrase inhibition

Standard StatusStandard

Sequence Length15 amino acids

Chemical FormulaC92H130N26O19

DescriptionStandard

        HFPRIWLHSLGQHIY
    

Molecular Weight1904.18 Da

Isoelectric Point (pI)8.77

Net Charge (pH 7.0)1.02

Net Charge (pH 7.4) 0.66

Charge Density (pH 7.0) 0.0680

GRAVY Index-0.21

Hydrophobic Moment 0.44

Boman Index0.20

Instability Index47.75

Aliphatic Index 104.00

Aromaticity 0.2000

Extinction Coeff. Reduced 6990.00

Extinction Coeff. Oxidized 6990.00

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

Amino Acid Composition

TPSA 709.21

LogP -2.16

H-bond Donors 25.0

H-bond Acceptors 23.0

Rotatable Bonds 56.0

Heavy Atoms 137.0

Ring Count 8.0

Amide Bonds 15.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0302212 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

Targetinhibition of disintegration catalyzed by integrase

Activity73 μM

MethodIC50

RECORD: Rec_0353260 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilyProtein-derived synthetic peptide

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

N-TermNone

C-TermNone

Bio-Activity Profile

Function

Antiviral Replication inhibition

Targetinhibition of strand transfer catalyzed by integrase

Activity41 μM

MethodIC50

Half-LifeMammalian: 3.5 h; Yeast: 10 min; E. coli: >10 h

PaperInhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). | Gleenberg IO, Herschhorn A, Hizi A. | J Mol Biol. 2007 Jun 22;369(5):1230-43. | DOI:10.1016/j.jmb.2007.03.073 | PMID:17490682 PMID17490682 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/17490682/

RECORD: Rec_0355458 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilyProtein-derived synthetic 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 Replication inhibition

TargetHIV-1

Activity187 μM

MethodIC50

Half-LifeMammalian: 3.5 h; Yeast: 10 min; E. coli: >10 h

PaperInhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr). | Gleenberg IO, Herschhorn A, Hizi A. | J Mol Biol. 2007 Jun 22;369(5):1230-43. | DOI:10.1016/j.jmb.2007.03.073 | PMID:17490682 PMID17490682 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/17490682/

RECORD: Rec_0386648 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:Inhibition of 3′-end processing catalyzed by integrase

Activity187 μM

MethodIC50

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