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Siamycin I
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Siamycin I is a tricyclic peptide antibiotic originally isolated from Streptomyces sp. AA6532. It exhibits antiviral and antibacterial effects against HIV and HSV, as well as B. subtilis, M. luteus and S. aureus.

Functional Peptides
Catalog number
CAS number
Molecular Formula
Molecular Weight
Siamycin I
(2S)-2-[[(2S)-2-[[(1S,4S,7S,13R,19S,22S,25S,28S,31R,36R,39S,45S,51S,54R,60S)-60-(2-amino-2-oxoethyl)-4-benzyl-25-[(2S)-butan-2-yl]-39-(hydroxymethyl)-19-[(4-hydroxyphenyl)methyl]-7,22-dimethyl-51-(2-methylpropyl)-2,5,8,11,14,17,20,23,26,29,38,41,44,47,50,53,56,59,62-nonadecaoxo-28,45-di(propan-2-yl)-33,34,64,65-tetrathia-3,6,9,12,15,18,21,24,27,30,37,40,43,46,49,52,55,58,61-nonadecazatricyclo[,54]hexahexacontane-31-carbonyl]amino]-3-phenylpropanoyl]amino]-3-(1H-indol-3-yl)propanoic acid
NP-06; siamycin II, Val(4)-; BMY 29304; FR 901724; N(1)Cys(2)-Leu-Gly-Val-Gly-Ser-Cys(3)-Asn-Asp(1)-Phe-Ala-Gly-Cys(2)-Gly-Tyr-Ala-Ile-Val-Cys(3)-Phe-Trp-OH; L-Tryptophan, L-Cysteinyl-L-leucylglycyl-L-valylglycyl-L-seryl-L-cysteinyl-L-asparaginyl-L-α-aspartyl-L-phenylalanyl-L-alanylglycyl-L-cysteinylglycyl-L-tyrosyl-L-alanyl-L-isoleucyl-L-valyl-L-cysteinyl-L-phenylalanyl-, cyclic(9→1)-peptide, cyclic(1→13),(7→19)-bis(disulfide)
Melting Point
255°C (dec.)
cyclo{CLGVGSCND}FAGCGYAIVCFW (Disulfide bridge: Cys1-Cys13, Cys7-Cys19)
Store at -20°C
Soluble in Methanol
InChI Key
Canonical SMILES
1. Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptide inhibitor siamycin I revealed through synchrotron radiation circular dichroism
Jiro Nakayama, Simon G Patching, Shalini Edara, Mary K Phillips-Jones, Giuliano Siligardi, Rohanah Hussain Phys Chem Chem Phys . 2013 Jan 14;15(2):444-7. doi: 10.1039/c2cp43722h.
The suitability of synchrotron radiation circular dichroism spectroscopy (SRCD) for studying interactions between the tricyclic peptide inhibitor siamycin I and the intact FsrC membrane sensor kinase in detergent micelles has been established. In the present study, tertiary structural changes demonstrate that inhibitor binding occurs at a different, non-overlapping site to the native ligand, GBAP.
2. Siamycin attenuates fsr quorum sensing mediated by a gelatinase biosynthesis-activating pheromone in Enterococcus faecalis
Emi Tanaka, Ritsuko Mitsuhata, Jiro Nakayama, Masaru Tanokura, Hiromi Kumon, Kenji Sonomoto, Yumi Uemura, Koji Nagata, Kenzo Nishiguchi, Reiko Kariyama J Bacteriol . 2007 Feb;189(4):1358-65. doi: 10.1128/JB.00969-06.
The expression of two Enterococcus faecalis virulence-related proteases, gelatinase (GelE) and serine protease (SprE), is positively regulated by a quorum-sensing system encoded by the fsr gene cluster. In this system, E. faecalis secretes an autoinducing peptide, gelatinase biosynthesis-activating pheromone (GBAP), which triggers the FsrC-FsrA two-component regulatory system controlling the expression of two transcripts, fsrBDC and gelE-sprE. In the present study, we screened actinomycete metabolites for inhibitors of fsr quorum sensing. E. faecalis was cultured with each actinomycete culture supernatant tested, and the production of gelatinase and the production of GBAP were examined using the first screening and the second screening, respectively. Culture supernatant of Streptomyces sp. strain Y33-1 had the most potent inhibitory effect on both gelatinase production and GBAP production without inhibiting E. faecalis cell growth. The inhibitor in the culture supernatant was identified as a known peptide antibiotic, siamycin I. Siamycin I inhibited both gelatinase production and GBAP production at submicromolar concentrations, and it inhibited E. faecalis cell growth at concentrations above micromolar concentrations. Quantitative analysis of fsrBDC and gelE-sprE transcripts revealed that siamycin I suppressed the expression of both transcripts at a sublethal concentration. Siamycin I attenuated gelatinase production even when an overdose of GBAP was exogenously added to the culture. These results suggested that siamycin I inhibited the GBAP signaling via the FsrC-FsrA two-component regulatory system in a noncompetitive manner. The sublethal concentrations of siamycin I also attenuated biofilm formation. Treatment with siamycin could be a novel means of treating enterococcal infections.
3. High-resolution solution structure of siamycin II: novel amphipathic character of a 21-residue peptide that inhibits HIV fusion
M S Friedrichs, T Furumai, M Tsunakawa, K L Constantine, R E Bruccoleri, S Hill, T Oki, M Nishio, H Ohkuma, D Detlefsen J Biomol NMR . 1995 Apr;5(3):271-86. doi: 10.1007/BF00211754.
The 21-amino acid peptides siamycin II (BMY-29303) and siamycin I (BMY-29304), derived from Streptomyces strains AA3891 and AA6532, respectively, have been found to inhibit HIV-1 fusion and viral replication in cell culture. The primary sequence of siamycin II is CLGIGSCNDFAGCGYAIVCFW. Siamycin I differs by only one amino acid; it 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. Siamycin II, when dissolved in a 50:50 mixture of DMSO and H2O, yields NOESY spectra with exceptional numbers of cross peaks for a peptide of this size. We have used 335 NOE distance constraints and 13 dihedral angle constraints to generate an ensemble of 30 siamycin II structures; these have average backbone atom and all heavy atom rmsd values to the mean coordinates of 0.24 and 0.52 A, respectively. The peptide displays an unusual wedge-shaped structure, with one face being predominantly hydrophobic and the other being predominantly hydrophilic. Chemical shift and NOE data show that the siamycin I structure is essentially identical to siamycin II. These peptides may 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 [Frèchet, D. et al. (1994) Biochemistry, 33, 42-50]. The amphipathic nature of siamycin II and siamycin I suggests that a polar (or apolar) site on the target protein may be masked by the apolar (or polar) face of the peptide upon peptide/protein complexation.

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