634182-11-9

Upstream product

• 73724-45-5 N-(9H-fluoren-9-ylmethoxycarbonyl)-L-serine 

Downstream Products

• 1094039-23-2 C₄₁H₅₂N₂O₈S 
• 1431429-96-7 C₄₀H₄₀N₄O₁₂S 
• 1431430-19-1 C₄₀H₄₀N₄O₁₂S 
• 1431430-12-4 C₄₁H₄₂N₄O₁₂S 
• 622832-88-6 Bis(Fmoc)-cystine 
• 1359740-82-1 (2S,3S)-methyl 2-(((benzyloxy)carbonyl)amino)-3-(((R)-2-(((benzyloxy)carbonyl)amino)-3-(tert-butoxy)-3-oxopropyl)thio)butanoate 
• 1359740-86-5 (2S,3S)-3-(((R)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-(tert-butoxy)-3-oxopropyl)thio)-2-(((benzyloxy)carbonyl)amino)butanoic acid 
• 1359014-82-6 (5S,6S,Z)-methyl 13-(9H-fluoren-9-yl)-6-methyl-3,11-dioxo-1-phenyl-2,12-dioxa-7-thia-4,10-diazatridec-8-ene-5-carboxylate 
• 1359014-81-5 1-O-methyl-3-methyl-7-S-phenyl-(2S,3S,6S)-N₂-(benzyloxycarbonyl)-N₆-(9H-fluoren-9-yl) lanthionate 
• 1359015-32-9 (2S,3S)-methyl 3-(((R)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-(tert-butoxy)-3-oxopropyl)thio)-2-(((benzyloxy)carbonyl)amino)butanoate 
• 682359-13-3 N-(9-fluorenylmethoxycarbonyl)-β-bromo-L-alanyl-L-alanine benzyl ester 
• 881996-32-3 (2R,6R)-N²,N⁶-bis(fluoren-9-ylmethoxycarbonyl)lanthionine α-allyl ester 
• 881996-33-4 (2R,6S)-N²,N⁶-bis(fluoren-9-ylmethoxycarbonyl)lanthionine α-allyl ester 
• 881995-79-5 (2R,6R)-N²,N⁶-bis(fluoren-9-ylmethoxycarbonyl)lanthionine α-tert-butyl ester 

Relevant academic research and scientific papers

Synthesis and Bioactivity of Diastereomers of the Virulence Lanthipeptide Cytolysin

Cytolysin, a two-component lanthipeptide comprising cytolysin S (CylLS″) and cytolysin L (CylLL″), is the only family member to exhibit lytic activity against mammalian cells in addition to synergistic antimicrobial activity. A subset of the thioether cross-links of CylLS″ and CylLL″ have ll stereochemistry instead of the canonical dl stereochemistry in all previously characterized lanthipeptides. The synthesis of a CylLS″ variant with dl stereochemistry is reported. Its antimicrobial activity was found to be decreased, but not its lytic activity against red blood cells. Hence, the unusual ll stereochemistry is not responsible for the lytic activity.

Synthesis of the antimicrobial S-Linked glycopeptide, glycocin F

The first total synthesis of glycocin F, a uniquely diglycosylated antimicrobial peptide bearing a rare S-linked N-acetylglucosamine (GlcNAc) moiety in addition to an O-linked GlcNAc, has been accomplished using a native chemical ligation strategy. The synthetic and naturally occurring peptides were compared by HPLC, mass spectrometry, NMR and CD spectroscopy, and their stability towards chymotrypsin digestion and antimicrobial activity were measured. This is the first comprehensive structural and functional comparison of a naturally occurring glycocin with an active synthetic analogue.

Lipolanthionine peptides act as inhibitors of TLR2-mediated IL-8 secretion. Synthesis and structure-activity relationships

Lipoproteins from Gram-positive and -negative bacteria, mycoplasma, and shorter synthetic lipopeptide analogues activate cells of the innate immune system via the Toll-like receptor TLR2/TLR1 or TLR2/TLR6 heterodimers. For this reason, these compounds constitute highly active adjuvants for vaccines either admixed or covalently linked. The lanthionine scaffold has structural similarity with the 5-(2,3-dihydroxypropyl)-cysteine core structure of the lipopeptides. Therefore, lanthionine-based lipopeptide amides were synthesized and probed for activity as potential TLR2 agonists or antagonists. A collection of analytically defined lipolanthionine peptide amides exhibited an inhibitory effect of the TLR2-mediated IL-8 secretion when applied in high molar excess to the agonistic synthetic lipopeptide Pam3Cys-Ser-(Lys)4-OH. Structure-activity relationships revealed the influence of the chirality of the two α-carbon atoms, the chain lengths of the attached fatty acids and fatty amines, and the oxidation level of the sulfur atom on the inhibitory activity of the lipolanthionine peptide amides.