145435-30-9

Upstream product

• 637-89-8 4-sulfanylphenol 
• 1073-72-9 4-hydroxythioanisole 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 2886-33-1 dibenzyl L-aspartate toluene-4-sulphonate 

Downstream Products

• 1105051-14-6 L-phenylalanine-L-aspartate dibenzylester 
• 1150657-35-4 C₂₇H₂₈N₂O₅*ClH 
• 1149740-79-3 C₄₈H₅₀N₄O₁₂ 

Relevant academic research and scientific papers

Alanine Scan of the Peptide Antibiotic Feglymycin: Assessment of Amino Acid Side Chains Contributing to Antimicrobial Activity

The antibiotic feglymycin is a linear 13-mer peptide synthesized by the bacterium Streptomyces sp. DSM 11171. It mainly consists of the nonproteinogenic amino acids 4-hydroxyphenylglycine and 3,5-dihydroxyphenylglycine. An alanine scan of feglymycin was performed by solution-phase peptide synthesis in order to assess the significance of individual amino acid side chains for biological activity. Hence, 13 peptides were synthesized from di- and tripeptide building blocks, and subsequently tested for antibacterial activity against Staphylococcus aureus strains. Furthermore we tested the inhibition of peptidoglycan biosynthesis enzymes MurA and MurC, which are inhibited by feglymycin. Whereas the antibacterial activity is significantly based on the three amino acids D-Hpg1, L-Hpg5, and L-Phe12, the inhibitory activity against MurA and MurC depends mainly on L-Asp13. The difference in the position dependence for antibacterial activity and enzyme inhibition suggests multiple molecular targets in the modes of action of feglymycin. à la mode scanning: An alanine scan of the peptide antibiotic feglymycin was performed by solution-phase peptide synthesis to assess the significance of individual amino acid side chains for its biological activity. Antibacterial activity against Staphylococcus aureus and the inhibition of enzymes MurA and MurC depend on different amino acids.

Total synthesis of the antiviral peptide antibiotic feglymycin

An adaptable approach: The first highly convergent stereoselective synthesis of feglymycin (see structure) and its enantiomer is based on the coupling of repeating peptide fragments. The use of weakly basic conditions throughout the synthesis suppressed t

Tryptophan-containing dipeptide derivatives as potent PPARγ antagonists: Design, synthesis, biological evaluation, and molecular modeling

The discovery of peroxisome proliferator-activated receptor γ (PPARγ) antagonists (also termed "selective PPARγ modulators, SPPARγM") is now of a great interest in the treatment of diabetes and obesity. The structure of compound 1a (G3335, Fig. 1), a novel class of PPARγ antagonist, is entirely different from that of other reported PPARγ antagonists. A series of 35 novel analogues (1b-l, 9a-d, 13a-t) were designed, synthesized and evaluated against the agonistic effects exerted by rosiglitazone. These results indicated that most functional groups of 1a were conserved, and six new compounds (1b, 1c, and 9a-d) exhibited strong PPARγ antagonistic activities (IC50 values of 5.2-25.8 μM) against 10 μM rosiglitazone in the promotion of the PPARγ-LBD-CBP (ligand-binding domain and cAMP-response-element binding protein) interaction as investigated by yeast two-hybrid technology based assay. Molecular modeling studies for compounds 1a-d, 1h, 9c-d, and 13a were also presented.

Peptide Synthesis in Aqueous Solution. V. Properties and Reactivities of (p-Hydroxyphenyl)benzylmethylsulfonium Salts for Direct Benzyl Esterification of N-Acylpeptides

Some (p-hydroxyphenyl)benzylmethylsulfonium salts were prepared. These compounds generated a benzyl cation and converted not only N-acylamino acids but also N-acylpeptides into their corresponding benzyl esters without causing the racemization.