94102-64-4

Usage

Uses

Used in Medical Research:
Tracheal cytotoxin, produced by Bordetella pertussis, is utilized as a research tool in the study of whooping cough and its effects on the respiratory system. Understanding the mechanisms by which this toxin damages ciliated epithelial cells can aid in the development of treatments and vaccines to combat pertussis.
Used in Vaccine Development:
Tracheal cytotoxin is used in the development of vaccines against whooping cough. By incorporating components of Bordetella pertussis, including the tracheal cytotoxin, vaccines can stimulate the immune system to recognize and respond to the bacterium, potentially reducing the severity of the disease or preventing infection altogether.
Used in Diagnostics:
Tracheal cytotoxin can be used as a biomarker in the diagnosis of whooping cough. Detection of the presence of this toxin in respiratory samples can help confirm the presence of Bordetella pertussis and assist in the timely initiation of appropriate treatment.
Used in Public Health Education:
Understanding the role of tracheal cytotoxin in the pathogenesis of whooping cough can be instrumental in public health education campaigns. Educating the public about the importance of vaccination and the role of Bordetella pertussis in causing respiratory distress can help increase vaccination rates and reduce the incidence of the disease.

Synthetic route

C80H93N7O22 → GlcNAc-(β1-4)-(anhydro)MurNAc-L-Ala-γ-D-Glu-meso-DAP-D-Ala (94102-64-4)

Conditions	Yield
With hydrogen; palladium(II) hydroxide In tetrahydrofuran under 14711.4 Torr; for 24h;	100%

C72H85N9O20 → GlcNAc-(β1-4)-(anhydro)MurNAc-L-Ala-γ-D-Glu-meso-DAP-D-Ala (94102-64-4)

Conditions	Yield
Stage #1: C72H85N9O20 With acetic acid at 80℃; for 2h; Inert atmosphere; Stage #2: With palladium on activated carbon; hydrogen at 20℃; for 18h; Inert atmosphere;	37 mg

Relevant academic research and scientific papers

From Genome to Proteome to Elucidation of Reactions for All Eleven Known Lytic Transglycosylases from Pseudomonas aeruginosa

An enzyme superfamily, the lytic transglycosylases (LTs), occupies the space between the two membranes of Gram-negative bacteria. LTs catalyze the non-hydrolytic cleavage of the bacterial peptidoglycan cell-wall polymer. This reaction is central to the growth of the cell wall, for excavating the cell wall for protein insertion, and for monitoring the cell wall so as to initiate resistance responses to cell-wall-acting antibiotics. The nefarious Gram-negative pathogen Pseudomonas aeruginosa encodes eleven LTs. With few exceptions, their substrates and functions are unknown. Each P. aeruginosa LT was expressed as a soluble protein and evaluated with a panel of substrates (both simple and complex mimetics of their natural substrates). Thirty-one distinct products distinguish these LTs with respect to substrate recognition, catalytic activity, and relative exolytic or endolytic ability. These properties are foundational to an understanding of the LTs as catalysts and as antibiotic targets.

Synthesis of diaminopimelic acid containing peptidoglycan fragments and tracheal cytotoxin (TCT) and investigation of their biological functions

Bacterial cell wall peptidoglycan (PGN) is a potent immunostimulator and immune adjuvant. The PGN of Gram-negative bacteria and some Gram-positive bacteria contain meso-diaminopimelic acid (meso-DAP), and we have recently shown that the intracellular protein Nodi is a PGN receptor and recognizes DAPcontaining peptides. In this study, we achieved the synthesis of DAP-containing PGN fragments, including the first chemical synthesis of tracheal cytotoxin (TCT), GlcNAc-(β1-4)-(anhydro) Mur-NAc-L-Ala-γ-D-Glu-meso- DAP-D-Ala, and a repeating-unit of DAP-type PGN, GlcNAc-(β1-4)-MurNAc-L- Ala-γ-D-Glu-meso-DAP-D-Ala. For the synthesis of PGN fragments, we first established a new synthetic method for an orthogonally protected meso-DAP derivative, and then we constructed the glycopeptide structures. The ability of these fragments to stimulate human Nodi, as well as differences in Nodi recognition of the variety of synthesized ligand structures were examined. The results showed that the substitution of the N terminus of iE-DAP is necessary for stronger Nodi recognition, but the structure of the substituent seems not to be strictly recognized. The importance of the carboxyl group at the 2-position of DAP for human Nod1 stimulation was also shown.