| Name
|
Indolicidin
|
| Other Name
|
ILPWKWPWWPWRR-NH2
|
| Sequence (Single letter abbreviations)
|
ILPWKWPWWPWRR-NH2
|
| Sequence（Three letter abbreviations）
|
{ILE}{LEU}{PRO}{TRP}{LYS}{TRP}{PRO}{TRP}{TRP}{PRO}{TRP}{ARG}{ARG}-NH2
|
| C-port
|
NH2
|
| Basic description
|
Indolicidin is a 13-residue peptide amide which was isolated and characterized from the cytoplasmic granules of bovine neutrophils, having potent antibacterial activity in vitro against bacteria and fungi. The primary structure of indolicidin is characterized by 5 tryptophan residues, which is the mole percentage of any known protein sequence and is unique among known endogenous antibacterial peptides.
|
| The molecular weight
|
1906.280
|
| Chemical formula
|
C100H132N26O13
|
| The purity
|
> 95%
|
| Storage conditions
|
Stored at -20°C. Keep tightly closed.
|
| Annotation
|
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| Documents
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| Figures
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| Reference
|
Shaw JE, et al. Mechanisms of antimicrobial peptide action: Studies of indolicidin assembly at model membrane interfaces by in situ atomic force microscopy. J. Struct. Biol. Apr 2006; 154(1):42-58.
Xing H, et al. Increased pathogen resistance and yield in transgenic plants expressing combinations of the modified antimicrobial peptides based on indolicidin and magainin. Planta. Apr 2006; 223(5): 1024-1032.
Hsu CH, et al. Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA. Nucleic Acids Res. Jul 2005; 33(13): 4053-4064.
|
Indolicidin
