Combining biocatalysis and chemoselective chemistries for glycopeptide antibiotics modification

• Published in: Current opinion in chemical biology Vol. 16; no. 1-2; pp. 170 - 178
• Main Authors: Li, Tsung-Lin, Liu, Yu-Chen, Lyu, Syue-Yi
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.04.2012
• Subjects: Anti-Bacterial Agents - chemistry; Anti-Bacterial Agents - metabolism; Antibiotics; Biocatalysis; Catalysis; Glycopeptides; Glycopeptides - chemistry; Glycopeptides - metabolism; Infection; Mutagenesis; Oxidation-Reduction; Pathogens; Protein engineering; Reviews
• ISSN: 1367-5931; 1879-0402
• DOI: 10.1016/j.cbpa.2012.01.017

► Glycopeptide antibiotics are classified into five subtypes. ► Sulfation modification of glycopeptide has been achieved using sulfotransferases. ► Naturally occurring glycopeptide was modified via aglycone and sugar exchanges. ► Glycopeptide analogs were amidated and aminated on a given sugar moiety. Glycopeptide antibiotics are clinically important medicines to treat serious Gram-positive bacterial infections. The emergence of glycopeptide resistance among pathogens has motivated considerable interest in expanding structural diversity of glycopeptide to counteract resistance. The complex structure of glycopeptide poses substantial barriers to conventional chemical methods for structural modifications. By contrast, biochemical approaches have attracted great attention because ample biosynthetic information and sophisticated toolboxes have been made available to change reaction specificity through protein engineering, domain swapping, pathway engineering, addition of substrate analogs, and mutagenesis.