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Anti-PqsR compounds as next-generation antibacterial agents against Pseudomonas aeruginosa: A review.
Soheili, Vahid; Tajani, Amineh Sadat; Ghodsi, Razieh; Bazzaz, Bibi Sedigheh Fazly.
Affiliation
  • Soheili V; Department of Pharmaceutical Control, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran.
  • Tajani AS; Department of Pharmaceutical Control, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran.
  • Ghodsi R; Department of Medicinal Chemistry, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran; Biotechnology Research Center, Pharmaceutical Institute, Mashhad University of Medical Sciences, Mashhad, Iran.
  • Bazzaz BSF; Department of Pharmaceutical Control, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran; Biotechnology Research Center, Pharmaceutical Institute, Mashhad University of Medical Sciences, Mashhad, Iran. Electronic address: FazliS@mums.ac.ir.
Eur J Med Chem ; 172: 26-35, 2019 Jun 15.
Article in En | MEDLINE | ID: mdl-30939351
Nowadays, due to spreading antibiotic resistance among clinically relevant pathogens, the requirement of novel therapeutic approaches is felt more than ever. One of the alternative strategies is anti-virulence therapy without affecting bacterial growth or viability. In Pseudomonas aeruginosa, an opportunistic human pathogen that exhibits intrinsic multi-drug resistance, both virulence factors' production and biofilm formation depends on its quorum sensing (QS) network. Therefore, targeting the key proteins involved in QS system is an attractive method to overcome P. aeruginosa pathogenicity and resistance. The transcriptional regulator PqsR, also called MvfR, is one of these major proteins which employs 3,4-dihydroxy-2-heptylquinoline (PQS) and 4-hydroxy-2-heptylquinoline (HHQ) as signaling molecules. Reviewing the advances in development of small molecules inhibit this protein, assist to open a new window to smart molecule design that may revolutionize treatment of P. aeruginosa infections.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Pseudomonas aeruginosa / Bacterial Proteins / Quinolones / Quinazolinones / Anti-Bacterial Agents Language: En Journal: Eur J Med Chem Year: 2019 Document type: Article Affiliation country: Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Pseudomonas aeruginosa / Bacterial Proteins / Quinolones / Quinazolinones / Anti-Bacterial Agents Language: En Journal: Eur J Med Chem Year: 2019 Document type: Article Affiliation country: Country of publication: