1149740-75-9Relevant academic research and scientific papers
Alanine Scan of the Peptide Antibiotic Feglymycin: Assessment of Amino Acid Side Chains Contributing to Antimicrobial Activity
H?nchen, Anne,Rausch, Saskia,Landmann, Benjamin,Toti, Luigi,Nusser, Antje,Süssmuth, Roderich D.
, p. 625 - 632 (2013/06/05)
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
Dettner, Frank,Haenchen, Anne,Schols, Dominique,Toti, Luigi,Nusser, Antje,Suessmuth, Roderick D.
supporting information; experimental part, p. 1856 - 1861 (2009/09/06)
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
