111505-52-3Relevant articles and documents
Hybrid Peptides Based on α-Aminoxy Acids as Antimicrobial and Anticancer Foldamers
Sinatra, Laura,Kolano, Lisa,Icker, Maik,Fritzsche, Stefan R.,Volke, Daniela,Gockel, Ines,Thieme, René,Hoffmann, Ralf,Hansen, Finn K.
, p. 827 - 835 (2021)
α-Aminoxy peptides represent an interesting group of peptidomimetics with high proteolytic stability and the ability to fold into specific, predictable secondary structures. Here, we present a series of hybrid peptides consisting of α-aminoxy acids and α-amino acids with cationic and aromatic, hydrophobic side chains in an alternating manner synthesized using an efficient protocol that combines solution- and solid-phase synthesis. 2D ROESY experiments with a representative hexamer suggested the presence of a 7/8 helical conformation in solution. Biological evaluation revealed a significant impact of the peptide chain length and the N-terminal cap on the antimicrobial and anticancer properties of this series of hybrid peptides. The Fmoc-capped peptide 6e displayed the most potent antimicrobial activity against a panel of Gram-negative and Gram-positive bacterial strains (e. g. against E. Coli: MIC=8 mg/L; S. aureus: MIC=4 mg/L).
Total synthesis of the antifungal depsipeptide petriellin A
Sleebs, Marianne M.,Scanlon, Denis,Karas, John,Maharani, Rani,Hughes, Andrew B.
, p. 6686 - 6693 (2011/10/18)
We report the solid-phase total synthesis of the antifungal highly modified cyclic depsipeptide petriellin A. The synthesis confirms earlier reports on the absolute configuration of the natural product. The solid-phase approach resulted in a protected lin
Serendipitous discovery of α-hydroxyalkyl esters as β-lactamase substrates
Pelto, Ryan B.,Pratt
experimental part, p. 10496 - 10506 (2011/10/18)
O-(1-Carboxy-1-alkyloxycarbonyl) hydroxamates were found to spontaneously decarboxylate in aqueous neutral buffer to form O-(2-hydroxyalkylcarbonyl) hydroxamates. While the former molecules do not react rapidly with serine β-lactamases, the latter are quite good substrates of representative class A and C, but not D, enzymes, and particularly of a class C enzyme. The enzymes catalyze hydrolysis of these compounds to a mixture of the α-hydroxy acid and hydroxamate. Analogous compounds containing aryloxy leaving groups rather that hydroxamates are also substrates. Structure-activity experiments showed that the α-hydroxyl group was required for any substantial substrate activity. Although both d- and l-α-hydroxy acid derivatives were substrates, the former were preferred. The response of the class C activity to pH and to alternative nucleophiles (methanol and d-phenylalanine) suggested that the same active site functional groups participated in catalysis as for classical substrates. Molecular modeling was employed to explore how the α-hydroxy group might interact with the class C β-lactamase active site. Incorporation of the α-hydroxyalkyl moiety into novel inhibitors will be of considerable interest.
3-Pyrroline-1-carbonyl (Pyroc) group: A removable protecting group for the kinetic resolution of racemic carboxylic acids and alcohols through catalytic asymmetric acylation
Sakakura, Akira,Umemura, Shuhei,Ishihara, Kazuaki
body text, p. 1647 - 1650 (2009/12/03)
The O-3-pyrroline-1-carbonyl (O-Pyroc) group and 3-pyrrolinamide are useful removable protecting groups for the kinetic resolution of racemic α-hydroxycarboxylic acids, β-hydroxycarboxylic acids, 1,2-dicarboxylic acids, and 1,2-diols using the L-histidine
STEREOCONTROLLED SYNTHESIS OF D-α-HYDROXY CARBOXYLIC ACIDS FROM L-AMINO ACIDS
Kunz, Horst,Lerchen, Hans-Georg
, p. 1873 - 1876 (2007/10/02)
Optically active D-α-hydroxy carboxylic acids are obtained from L-amino acids via L-α-halocarboxylic acids and their stereoselective reaction with cesium p-nitrobenzoate.
