775276-56-7Relevant academic research and scientific papers
An improved solid-phase methodology for the synthesis of putative hexa- and heptapeptide intermediates in vancomycin biosynthesis
Li, Dong Bo,Robinson, John A.
, p. 1233 - 1239 (2005)
The biosynthesis of the vancomycin aglycone involves three oxidative phenol coupling reactions, each catalyzed by a discrete cytochrome P450-like enzyme. Studies on the mechanism and specificity of the enzyme (called OxyB) catalyzing the first coupling, require access to suitable linear peptide precursors, each conjugated as a thioester to a peptide carrier domain of the vancomycin non-ribosomal peptide synthetase. An efficient route to representative free linear peptides is described here. The method makes use of Alloc-chemistry during solid-phase assembly of the peptide backbone, but importantly and in contrast to earlier efforts, largely avoids the use of amino acid side chain protecting groups. In this way, the target linear peptides can be released directly from the solid support under very mild conditions. The Royal Society of Chemistry 2005.
Synthetic studies towards Pseudoxylallemycin B, an antibiotic active against gram-negative bacteria: Total synthesis of 3-epi-Pseudoxylallemycin B
Gunjal, Vidya B.,Reddy, D. Srinivasa
supporting information, p. 2900 - 2903 (2018/06/25)
In an attempt towards the total synthesis of Pseudoxylallemycin B, a homo dimeric, N-methylated macrocyclic tetrapeptidic natural product, synthesis of its epimer at position 3 (D-Tyr instead of L-Tyr) is described here. During the course of synthesis we came across a striking yet unusual observation of complete epimerization which led to the formation of 3-epi-Pseudoxylallemycin B.
