Synthesis of 4-fluorinated UDP-MurNAc pentapeptide as an inhibitor of bacterial growth.

Org Lett

Bio-Macromolecular Chemistry Lab, Division of Biological Sciences, Graduate School of Science, Frontier Research Center for Post-Genomic Science and Technology, Hokkaido University, Kita 21, Nishi 11, Sapporo 001-0021 Japan.

Published: May 2004

AI Article Synopsis

Article Abstract

4-Fluorinated UDP-MurNAc pentapeptide, 2, has been synthesized. In our previous study, UDP-MurNAc pentapeptide analogue 1 was found to be incorporated into the bacterial cell wall through biosynthesis. Compound 2 showed growth-inhibition activity against Gram-positive bacteria when it was added to growth media at 0.01 mg/mL. [structure--see text]

Download full-text PDF

Source
http://dx.doi.org/10.1021/ol049598wDOI Listing

Publication Analysis

Top Keywords

udp-murnac pentapeptide
12
4-fluorinated udp-murnac
8
synthesis 4-fluorinated
4
pentapeptide inhibitor
4
inhibitor bacterial
4
bacterial growth
4
growth 4-fluorinated
4
pentapeptide synthesized
4
synthesized previous
4
previous study
4

Similar Publications

Anti-Tuberculosis Mur Inhibitors: Structural Insights and the Way Ahead for Development of Novel Agents.

Pharmaceuticals (Basel)

March 2023

Department of Chemistry and Biochemistry, The Novel Drug and Vaccine Delivery Systems Facility, Laurentian University, Sudbury, ON P3E 2C6, Canada.

Mur enzymes serve as critical molecular devices for the synthesis of UDP-MurNAc-pentapeptide, the main building block of bacterial peptidoglycan polymer. These enzymes have been extensively studied for bacterial pathogens such as and . Various selective and mixed Mur inhibitors have been designed and synthesized in the past few years.

View Article and Find Full Text PDF

Cell wall glycopolymers (CWPGs) in Gram-positive bacteria have been reported to be involved in several bacterial processes. These polymers, pillars for proteins and S-layer, are essential for the bacterial surface setup, could be essential for growth, and, in pathogens, participate most often in virulence. CWGPs are covalently anchored to peptidoglycan by proteins that belong to the LytR-CpsA-PSr (LCP) family.

View Article and Find Full Text PDF

A Fungal Defensin Inhibiting Bacterial Cell-Wall Biosynthesis with Non-Hemolysis and Serum Stability.

J Fungi (Basel)

February 2022

Group of Peptide Biology and Evolution, State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, 1 Beichen West Road, Chaoyang District, Beijing 100101, China.

Defensins are a class of cationic disulfide-bridged antimicrobial peptides (AMPs) present in many eukaryotic organisms and even in bacteria. They primarily include two distinct but evolutionarily related superfamilies ( and ). Defensins in fungi belong to the members of the -superfamily with the cysteine-stabilized α-helical and β-sheet fold.

View Article and Find Full Text PDF

Lipid II, the main component of the bacterial cell wall, is synthesized by the addition of UDP--acetylglucosamine to the UDP--acetylmuramic acid pentapeptide catalyzed by the glycosyltransferase MurG. Owing to its critical role in cell-wall biosynthesis, MurG is considered to be an attractive target for antibacterial agents. Although the Mur family ligases have been extensively studied, the molecular mechanism of the oligomeric scaffolding assembly of MurG remains unclear.

View Article and Find Full Text PDF

Discovery of novel antibacterial agents: Recent developments in D-alanyl-D-alanine ligase inhibitors.

Chem Biol Drug Des

September 2021

Department of Pharmacy, Henan Provincial People's Hospital, Zhengzhou University People's Hospital, Henan University People's Hospital, Zhengzhou, China.

Bacterial infections can cause serious problems that threaten public health over a long period of time. Moreover, the continuous emergence of drug-resistant bacteria necessitates the development of novel antibacterial agents. D-alanyl-D-alanine ligase (Ddl) is an indispensable adenosine triphosphate-dependent bacterial enzyme involved in the biosynthesis of peptidoglycan precursor, which catalyzes the ligation of two D-alanine molecules into one D-alanyl-D-alanine dipeptide.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!