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General Information
DRAVP ID DRAVPe02302
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
Assay Antiviral Assay
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity No cytotoxicity information found in the reference(s) presented
Binding Target Not Found
Mechanism These peptides act by preventing oligomerization of the HIV transmembrane glycoprotein gp41, or by interfering with interactions between gp41 and the envelope glycoprotein gp120, the cell membrane or membrane-bound proteins.binding siamycin II or siamycin I may play a crucial role in blocking interactions between HIV and the T-cell surface, an essential step in the fusion process.
Structure Information
PDB ID None
Linear/Cyclic Cyclic
N-terminal Modification Amidation
C-terminal Modification Free
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).
Stereochemistry L
Physicochemical Information
Formula C98H139N23O27S4
Absent amino acids EHKMOPQRTU
Common amino acids CG
Mass 2199.56
Pl 3.8
Basic residues 0
Acidic residues 1
Hydrophobic residues 9
Net charge -1
Boman Index -0.98
Hydrophobicity 1.171
Aliphatic Index 79.05
Half Life
Extinction Coefficient cystines 7240
Absorbance 280nm 3.292
Polar residues 8
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 ournal 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).
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.