DRAVP ID  DRAVPe00739

Peptide Name   SAH-gp41(626-662) B

Sequence  XTWMEWDREINNYTSLIHSLIEESQNQXEKNXQELLE

Sequence Length  37

UniProt ID  P04582 

Taxon ID  None

Source  Synthetic construct

Validation   Experimentally Validated

Gene Name/ID  Not Available

GenBank  Not Available

Amino Acid position  Not Available

Domain Accession ID  Not Available

Nucleotide sequence ID  Not Available

Molecular Type  Not Available

Chromosomal Position  Not Available

Target Organism  HIV

Assay  luciferase assay

Activity 

• [Ref.20660316]HIV-1 HxB2:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=4.5±1.4 nM);
• HIV-1 YU2:inhibition of virus infection in Cf2Th-CD4-CCR5 cells(IC50=1958±259 nM).

Hemolytic Activity  No hemolysis information or data found in the reference(s) presented in this entry

Cytotoxicity 

• No cytotoxicity information or data found in the reference(s) presented in this entry

Binding Target  Not found

Mechanism  The peptide disrupts assembly of the six-helix bundle viral fusion apparatus by mimicking the heptad repeat 2 (HR2) oligomerization domain of the gp41 envelope glycoprotein.

PDB ID  None

Predicted Structure Download  No predicted structure available

Linear/Cyclic  Cyclic

N-terminal Modification  Free

C-terminal Modification  Free

Other Modification  The 'X' at position 1 indicates Norleucine,the 'X' at position 28,32 indicates S-2-(4'-pentenyl) alanine. X(28) and X (32) are cross-linked by hydrocarbon stapling.

Stereochemistry  L

Literature 1

Title   Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic.

Pubmed ID   20660316

Reference   Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14093-8.

Author   Bird GH, Madani N, Perry AF, Princiotto AM, Supko JG, He X, Gavathiotis E, Sodroski JG, Walensky LD.

DOI   10.1073/pnas.1002713107