General Information


DRAVP ID  DRAVPe00738

Peptide Name   SAH-gp41(626-662)A

Sequence  XTWXEWDXEINNYTSLIHSLIEESQNQQEKNEQELLE

Sequence Length  37

UniProt ID  P04582 

Source  Synthetic construct



Activity Information


Target Organism  HIV

Assay  luciferase assay

Activity 

  • [Ref.20660316]HIV-1 HxB2:inhibition of virus infection in Cf2Th-CD4-CXCR4 cells(IC50=2.1±0.3 nM);
  • HIV-1 YU2:inhibition of virus infection in Cf2Th-CD4-CCR5 cells(IC50=339±162 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.



Structure Information


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 4,8 indicates S-2-(4'-pentenyl) alanine. X(4) and X (5) are cross-linked by hydrocarbon stapling.

Stereochemistry  L



Physicochemical Information


Formula  C182H267N47O64

Absent amino acids  ACFGMPRV

Common amino acids  E

Mass  4525.44

Pl  3.93

Basic residues  2

Acidic residues  9

Hydrophobic residues  9

Net charge  -7

Boman Index  -9851

Hydrophobicity  -121.08

Aliphatic Index  73.78

Half Life 

  •     Mammalian:
  •     Yeast:
  •     E.coli:

Extinction Coefficient cystines  12490

Absorbance 280nm  346.94

Polar residues  10



Literature Information


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