84668-69-9Relevant 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.
Polymorphism of amino acid-based dendrons: From organogels to microcrystals
Kuang, Gui-Chao,Teng, Ming-Jun,Jia, Xin-Ru,Chen, Er-Qiang,Wei, Yen
, p. 1163 - 1170 (2011/12/15)
There is a delicate balance for a low-weight molecule to behave as a gelator or crystal. The synthesis of two novel amino acid-based naphthalene-dendrons, Nap-G1 and Nap-G2 is described. Both dendrons display polymorphic properties in organic solvents. Nap-G1 developed a fibrous network with β-sheet architecture in cyclohexane but exhibited a spherulitic network in mixed solvents (chloroform/petroleum ether 1:5, v/v). On the other hand, Nap-G2 acted as an efficient organogelator in chloroform but formed crystalline fibers in relatively high polarity solvents (such as acetone and methanol). Combinations of characterizations have been employed to study the polymorphism. In the balance: Two amino acid-based naphthalene-dendrons display different polymorphic properties in organic solvents. Nap-G1 developed a fibrous network with β-sheet architecture in cyclohexane but exhibited a spherulitic network in mixed solvents while Nap-G2 acts as an efficient organogelator in chloroform but formed crystalline fibers in relatively high polarity solvents (see picture).
Carbonic anhydrase activators: Human isozyme II is strongly activated by oligopeptides incorporating the carboxyterminal sequence of the bicarbonate anion exchanger AE1
Scozzafava, Andrea,Supuran, Claudiu T.
, p. 1177 - 1180 (2007/10/03)
Di-/tri- and especially tetrapeptides incorporating the sequence DADD present in the carboxyterminal region of the bicarbonate/chloride anion exchanger AE1 strongly activate human carbonic anhydrase (CA) isozyme II, whereas they act as more inefficient ac
