Paquette, Andre R. published the artcileRpoN-Based stapled peptides with improved DNA binding suppress Pseudomonas aeruginosa virulence, Application In Synthesis of 71989-31-6, the publication is RSC Medicinal Chemistry (2022), 13(4), 445-455, database is CAplus and MEDLINE.
Stapled peptides have the ability to mimic ¦Á-helixes involved in protein binding and have proved to be effective pharmacol. agents for disrupting protein-protein interactions. DNA-binding proteins such as transcription factors bind their cognate DNA sequences via an ¦Á-helix interacting with the major groove of DNA. We previously developed a stapled peptide based on the bacterial alternative sigma factor RpoN capable of binding the RpoN DNA promoter sequence and inhibiting RpoN-mediated expression in Escherichia coli. We have elucidated a structure-activity relationship for DNA binding by this stapled peptide, improving DNA binding affinity constants in the high nM range. Lead peptides were shown to have low toxicity as determined by their low hemolytic activity at 100 ¦ÌM and were shown to have anti-virulence activity in a Galleria mellonella model of Pseudomonas aeruginosa infection. These findings support further preclin. development of stapled peptides as antivirulence agents targeting P. aeruginosa.
RSC Medicinal Chemistry published new progress about 71989-31-6. 71989-31-6 belongs to catalysis-chemistry, auxiliary class Amino acide derivatives,pyrrolidine, name is Fmoc-Pro-OH, and the molecular formula is C20H19NO4, Application In Synthesis of 71989-31-6.
Referemce:
https://courses.lumenlearning.com/boundless-chemistry/chapter/catalysis/,
Catalysis – Wikipedia