General Information
-
DRAMP ID
- DRAMP30385
-
Peptide Name
- MT-WQ-IDL(626-656)
-
Source
- Synthetic construct
-
Family
- Retroviridae
-
Gene
- Not found
-
Sequence
- MTWEEWDKKIEEYTKKIEELIKKSQNQQIDL
-
Sequence Length
- 31
-
UniProt Entry
- P04578
-
Protein Existence
- Not found
Activity Information
-
Biological Activity
- Antimicrobial, Antiviral
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Target Organism
-
- [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=0.6±0.1 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=1.2± 0.2 nM);
- HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=0.6 ±0.1 nM);
- HIV-1 clinical isolates(8 clinical isolates):inhibition of virus infection in MT-2 cells(IC50=0.5-15.1 nM);
- HIV-1 pseudoviruses(7 pseudoviruses):inhibition of pseudoviruses infection in MT-2 cells(IC50=0.1-9.0 nM);
- HIV-1 T20-resistant strains(5 strains):inhibition of virus infection in MT-2 cells(IC50=0.1-4.4 nM);
- HIV-1 T2635-resistant strain(6 strains):inhibition of virus infection in MT-2 cells(IC50=1.1-11.3 nM).
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Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
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Cytotoxicity
- No cytotoxicity information found in the reference(s) presented
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Binding Target
- membrane
Structure Information
-
Linear/Cyclic
- Linear
-
N-terminal Modification
- Free
-
C-terminal Modification
- Free
-
Nonterminal Modifications and Unusual Amino Acids
- None
-
Stereochemistry
- L
-
Structure
- Not found
-
Structure Description
- Not found
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Helical Wheel Diagram
-
PDB ID
- None
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Predicted Structure
- There is no predicted structure for DRAMP30385.
Physicochemical Information
-
Formula
- C176H279N43O56S
Absent Amino Acids
- ACFGHPRV
Common Amino Acids
- EK
Mass
- 3925.47
PI
- 4.86
Basic Residues
- 6
Acidic Residues
- 8
Hydrophobic Residues
- 8
Net Charge
- -2
-
Boman Index
- -8701
Hydrophobicity
- -1.394
Aliphatic Index
- 75.48
Half Life
-
- Mammalian:30 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 12490
Absorbance 280nm
- 416.33
Polar Residues
- 5
DRAMP30385
Comments Information
Mechanism
- The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation.
Literature Information
- ·Literature 1
-
Title
- Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.
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Pubmed ID
- 27795416
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Reference
- J Virol. 2016 Dec 16;91(1):e01445-16.
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Author
- Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.