To the extent possible under law, the person who associated CC0 with this work has waived all copyright and related or neighboring rights to this work.
General Information
DRAVP ID DRAVPe02250
Peptide Name Siamycin II
Sequence CLGIGSCNDFAGCGYAIVCFW
Sequence Length 21
UniProt ID No entry found
Taxon ID None
Source Streptomyces strains AA3891
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-1
Assay CPEb (XTT)
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity
Binding Target as an inhibitor of fusion of gp160- and CD4-expressing cell
Mechanism Siamycin I inhibits fusion between C8166 cells and CEM-SS cells chronically infected with HIV (50% effective dose of 0.08 microM) but has no effect on Sendai virus-induced fusion or murine myoblast fusion.
Structure Information
PDB ID None
Linear/Cyclic Linear
N-terminal Modification Free
C-terminal Modification Amidation
Other Modification It differs from Siamycin I only by one amino acid. Siamycin I has a valine residue at position 4. In both peptides, disulfide bonds link Cys1 with Cys13 and Cys7 with Cys19, and the side chain of Asp9 forms an amide bond with the N-terminus (XXJ). The original has been replaced since antimicrobial assays revealed no activity.
Stereochemistry L
Physicochemical Information
Formula C98H139N23O27S4
Absent amino acids EHKMPQRT
Common amino acids CG
Mass 2199.56
Pl 3.8
Basic residues 0
Acidic residues 1
Hydrophobic residues 9
Net charge -1
Boman Index 2.069
Hydrophobicity 1.171
Aliphatic Index 79.05
Half Life
Extinction Coefficient cystines 7240
Absorbance 280nm 362
Polar residues 11
Literature Information
Literature 1
Title High-resolution solution structure of siamycin II: novel amphipathic character of a 21-residue peptide that inhibits HIV fusion;
Pubmed ID 7787424
Reference Journal of biomolecular NMR, 5(3), 271–286;
Author Constantine, K. L., Friedrichs, M. S., Detlefsen, D., Nishio, M., Tsunakawa, M., Furumai, T., Ohkuma, H., Oki, T., Hill, S., & Bruccoleri, R. E. (1995);
Literature 2
Title Siamycins I and II, new anti-HIV peptides: I. Fermentation, isolation, biological activity and initial characterization
Pubmed ID 7797448
Reference The Journal of antibiotics, 48(5), 433–434.
Author Tsunakawa, M., Hu, S. L., Hoshino, Y., Detlefson, D. J., Hill, S. E., Furumai, T., White, R. J., Nishio, M., Kawano, K., & Yamamoto, S. (1995).
To the extent possible under law, the person who associated CC0 with this work has waived all copyright and related or neighboring rights to this work.