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Antibacterial properties of the pituitary adenylate cyclase-activating polypeptide: A new human antimicrobial peptide
by
Iddir, Mustapha
, Debbabi, Somia
, Groleau, Marie-Christine
, Chatenet, David
, Létourneau, Myriam
, Doucet, Nicolas
, Narayanan, Chitra
, Gosselin, Laura-Lee
, Gagnon, Jacinthe
, Déziel, Eric
in
Amino acids
/ Analogs
/ Animals
/ Anti-Bacterial Agents - chemistry
/ Anti-Bacterial Agents - pharmacology
/ Antibiotics
/ Antimicrobial agents
/ Bacteria
/ Biology and Life Sciences
/ Burkholderia cenocepacia
/ Burkholderia cepacia complex - growth & development
/ Chemical compounds
/ CHO Cells
/ Conformation
/ Cricetulus
/ Cystic fibrosis
/ E coli
/ Humans
/ Hydration
/ Life Sciences
/ Medicine and Health Sciences
/ Metabolites
/ Multidrug resistant organisms
/ Neuroprotection
/ Pharmacology
/ Physical Sciences
/ Pituitary adenylate cyclase-activating polypeptide
/ Pituitary Adenylate Cyclase-Activating Polypeptide - chemistry
/ Pituitary Adenylate Cyclase-Activating Polypeptide - pharmacology
/ Polypeptides
/ Protein Structure, Secondary
/ Research and Analysis Methods
/ Simulation
2018
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Antibacterial properties of the pituitary adenylate cyclase-activating polypeptide: A new human antimicrobial peptide
by
Iddir, Mustapha
, Debbabi, Somia
, Groleau, Marie-Christine
, Chatenet, David
, Létourneau, Myriam
, Doucet, Nicolas
, Narayanan, Chitra
, Gosselin, Laura-Lee
, Gagnon, Jacinthe
, Déziel, Eric
in
Amino acids
/ Analogs
/ Animals
/ Anti-Bacterial Agents - chemistry
/ Anti-Bacterial Agents - pharmacology
/ Antibiotics
/ Antimicrobial agents
/ Bacteria
/ Biology and Life Sciences
/ Burkholderia cenocepacia
/ Burkholderia cepacia complex - growth & development
/ Chemical compounds
/ CHO Cells
/ Conformation
/ Cricetulus
/ Cystic fibrosis
/ E coli
/ Humans
/ Hydration
/ Life Sciences
/ Medicine and Health Sciences
/ Metabolites
/ Multidrug resistant organisms
/ Neuroprotection
/ Pharmacology
/ Physical Sciences
/ Pituitary adenylate cyclase-activating polypeptide
/ Pituitary Adenylate Cyclase-Activating Polypeptide - chemistry
/ Pituitary Adenylate Cyclase-Activating Polypeptide - pharmacology
/ Polypeptides
/ Protein Structure, Secondary
/ Research and Analysis Methods
/ Simulation
2018
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Antibacterial properties of the pituitary adenylate cyclase-activating polypeptide: A new human antimicrobial peptide
by
Iddir, Mustapha
, Debbabi, Somia
, Groleau, Marie-Christine
, Chatenet, David
, Létourneau, Myriam
, Doucet, Nicolas
, Narayanan, Chitra
, Gosselin, Laura-Lee
, Gagnon, Jacinthe
, Déziel, Eric
in
Amino acids
/ Analogs
/ Animals
/ Anti-Bacterial Agents - chemistry
/ Anti-Bacterial Agents - pharmacology
/ Antibiotics
/ Antimicrobial agents
/ Bacteria
/ Biology and Life Sciences
/ Burkholderia cenocepacia
/ Burkholderia cepacia complex - growth & development
/ Chemical compounds
/ CHO Cells
/ Conformation
/ Cricetulus
/ Cystic fibrosis
/ E coli
/ Humans
/ Hydration
/ Life Sciences
/ Medicine and Health Sciences
/ Metabolites
/ Multidrug resistant organisms
/ Neuroprotection
/ Pharmacology
/ Physical Sciences
/ Pituitary adenylate cyclase-activating polypeptide
/ Pituitary Adenylate Cyclase-Activating Polypeptide - chemistry
/ Pituitary Adenylate Cyclase-Activating Polypeptide - pharmacology
/ Polypeptides
/ Protein Structure, Secondary
/ Research and Analysis Methods
/ Simulation
2018
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Antibacterial properties of the pituitary adenylate cyclase-activating polypeptide: A new human antimicrobial peptide
Journal Article
Antibacterial properties of the pituitary adenylate cyclase-activating polypeptide: A new human antimicrobial peptide
2018
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Overview
The Pituitary Adenylate Cyclase-Activating Polypeptide (PACAP), a polycationic, amphiphilic and helical neuropeptide, is well known for its neuroprotective actions and cell penetrating properties. In the present study, we evaluated the potent antibacterial property of PACAP38 and related analogs against various bacterial strains. Interestingly, PACAP38 and related analogs can inhibit the growth of various bacteria including Escherichia coli (JM109), Bacillus subtilis (PY79), and the pathogenic Burkholderia cenocepacia (J2315). Investigation of the mechanism of action suggested that a PACAP metabolite, identified as PACAP(9-38), might indeed be responsible for the observed PACAP38 antibacterial action. Surprisingly, PACAP(9-38), which does not induce haemolysis, exhibits an increased specificity toward Burkholderia cenocepacia J2315 compared to other tested bacteria. Finally, the predisposition of PACAP(9-38) to adopt a π-helix conformation rather than an α-helical conformation like PACAP38 could explain this gain in specificity. Overall, this study has revealed a new function for PACAP38 and related derivatives that can be added to its pleiotropic biological activities. This innovative study could therefore pave the way toward the development of new therapeutic agents against multiresistant bacteria, and more specifically the Burkholderia cenocepacia complex.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ Analogs
/ Animals
/ Anti-Bacterial Agents - chemistry
/ Anti-Bacterial Agents - pharmacology
/ Bacteria
/ Burkholderia cepacia complex - growth & development
/ E coli
/ Humans
/ Medicine and Health Sciences
/ Multidrug resistant organisms
/ Pituitary adenylate cyclase-activating polypeptide
/ Pituitary Adenylate Cyclase-Activating Polypeptide - chemistry
/ Pituitary Adenylate Cyclase-Activating Polypeptide - pharmacology
/ Protein Structure, Secondary
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