General Information
DRAVP ID DRAVPe02275
Peptide Name Maculatin 1.1
Sequence GLFVGVLAKVAAHVVPAIAEHF
Sequence Length 22
UniProt ID No entry found
Taxon ID None
Source Skin secretions, Litoria genimaculate, Litoria eucnemis, Australia
Validation Experimentally Validated
Origin Information
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
Activity Information
Target Organism HIV
Assay HIV infection and cell viability assay
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity
Binding Target Envelope/outer leaflet of the membrane
Mechanism Maculatin 1.1 is an amphibian-derived antimicrobial peptide that demonstrates potent inhibitory effects on HIV infection and transmission. It prevents HIV by disrupting the viral envelope, a critical structure required for viral fusion with target cells. When preincubated with the virus, maculatin 1.1 effectively blocks viral fusion, thereby preventing the virus from entering T cells. This peptide also exhibits the remarkable ability to inhibit the transfer of HIV from dendritic cells (DCs) to T cells, even when DCs are exposed to the peptide up to eight hours after capturing the virus. By accessing and destroying DC-sequestered HIV, maculatin 1.1 halts the progression of infection. These properties, coupled with its non-toxic effects on target cells, suggest that maculatin 1.1 holds significant promise as a topical inhibitor for mucosal HIV transmission and provides a novel approach to understanding the complex mechanisms of HIV capture and transfer by DCs.
Structure Information
PDB ID None
Linear/Cyclic Linear
N-terminal Modification Free
C-terminal Modification Free
Other Modification None
Stereochemistry L
Physicochemical Information
Formula C108H169N27O25
Absent amino acids CDMNOQRSTUWY
Common amino acids AV
Mass 2245.7
Pl 6.92
Basic residues 1
Acidic residues 1
Hydrophobic residues 15
Net charge 0
Boman Index -1.37
Hydrophobicity 1.432
Aliphatic Index 141.82
Half Life
Extinction Coefficient cystines 0
Absorbance 280nm 0
Polar residues 4
Literature Information
Literature 1
Title Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells
Pubmed ID 16140737
Reference Journal of virology, 79(18), 11598–11606.
Author VanCompernolle, S. E., Taylor, R. J., Oswald-Richter, K., Jiang, J., Youree, B. E., Bowie, J. H., Tyler, M. J., Conlon, J. M., Wade, D., Aiken, C., Dermody, T. S., KewalRamani, V. N., Rollins-Smith, L. A., & Unutmaz, D. (2005)