Comparative functional properties of engineered cationic antimicrobial peptides consisting exclusively of tryptophan and either lysine or arginine.
Identifieur interne : 001329 ( Main/Exploration ); précédent : 001328; suivant : 001330Comparative functional properties of engineered cationic antimicrobial peptides consisting exclusively of tryptophan and either lysine or arginine.
Auteurs : Berthony Deslouches [États-Unis] ; Mary L. Hasek [États-Unis] ; Jodi K. Craigo [États-Unis] ; Jonathan D. Steckbeck [États-Unis] ; Ronald C. Montelaro [États-Unis]Source :
- Journal of medical microbiology [ 1473-5644 ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Antimicrobial Cationic Peptides, Arginine, Lysine, Tryptophan.
- chemical , pharmacology : Antimicrobial Cationic Peptides.
- drug effects : Macrophages, Pseudomonas aeruginosa.
- Drug Resistance, Multiple, Bacterial, Humans, Protein Binding.
Abstract
We previously reported a series of de novo engineered cationic antibiotic peptides (eCAPs) consisting exclusively of arginine and tryptophan (WR) that display potent activity against diverse multidrug-resistant (MDR) bacterial strains. In this study, we sought to examine the influence of arginine compared to lysine on antibacterial properties by direct comparison of the WR peptides (8-18 residues) with a parallel series of engineered peptides containing only lysine and tryptophan. WR and WK series were compared for antibacterial activity by bacterial killing and growth inhibition assays and for mechanism of peptide-bacteria interactions by surface plasmon resonance and flow cytometry. Mammalian cytotoxicity was also assessed by flow cytometry, haemolytic and tetrazolium-based assays. The shortest arginine-containing peptides (8 and 10 mers) displayed a statistically significant increase in activity compared to the analogous lysine-containing peptides. The WR and WK peptides achieved maximum antibacterial activity at the 12-mer peptide (WK12 or WR12). Further examination of antibacterial mechanisms of the optimally active 12-mer peptides using surface plasmon resonance and flow cytometry demonstrates stronger interactions with Pseudomonasaeruginosa, greater membrane permeabilizing activity, and lower inhibitory effects of divalent cations on activity and membrane permeabilization properties of WR12 compared to WK12 (P < 0.05). Importantly, WK12 and WR12 displayed similar negligible haemolytic and cytotoxic effects at peptide concentrations up to ten times the MIC or 20 times the minimum bactericidal concentration. Thus, arginine, compared to lysine, can indeed yield enhanced antibacterial activity to minimize the required length to achieve functional antimicrobial peptides.
DOI: 10.1099/jmm.0.000258
PubMed: 27046192
Affiliations:
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Hasek</name><affiliation wicri:level="2"><nlm:affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA</wicri:regionArea><placeName><region type="state">Pennsylvanie</region></placeName></affiliation></author><author><name sortKey="Craigo, Jodi K" sort="Craigo, Jodi K" uniqKey="Craigo J" first="Jodi K" last="Craigo">Jodi K. Craigo</name><affiliation wicri:level="2"><nlm:affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA</wicri:regionArea><placeName><region type="state">Pennsylvanie</region></placeName></affiliation></author><author><name sortKey="Steckbeck, Jonathan D" sort="Steckbeck, Jonathan D" uniqKey="Steckbeck J" first="Jonathan D" last="Steckbeck">Jonathan D. 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Montelaro</name><affiliation wicri:level="2"><nlm:affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA</wicri:regionArea><placeName><region type="state">Pennsylvanie</region></placeName></affiliation></author></analytic><series><title level="j">Journal of medical microbiology</title><idno type="eISSN">1473-5644</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antimicrobial Cationic Peptides (chemistry)</term><term>Antimicrobial Cationic Peptides (pharmacology)</term><term>Arginine (chemistry)</term><term>Drug Resistance, Multiple, Bacterial</term><term>Humans</term><term>Lysine (chemistry)</term><term>Macrophages (drug effects)</term><term>Protein Binding</term><term>Pseudomonas aeruginosa (drug effects)</term><term>Tryptophan (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arginine ()</term><term>Humains</term><term>Liaison aux protéines</term><term>Lysine ()</term><term>Macrophages ()</term><term>Multirésistance bactérienne aux médicaments</term><term>Peptides antimicrobiens cationiques ()</term><term>Peptides antimicrobiens cationiques (pharmacologie)</term><term>Pseudomonas aeruginosa ()</term><term>Tryptophane ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antimicrobial Cationic Peptides</term><term>Arginine</term><term>Lysine</term><term>Tryptophan</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antimicrobial Cationic Peptides</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Macrophages</term><term>Pseudomonas aeruginosa</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Peptides antimicrobiens cationiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Drug Resistance, Multiple, Bacterial</term><term>Humans</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Arginine</term><term>Humains</term><term>Liaison aux protéines</term><term>Lysine</term><term>Macrophages</term><term>Multirésistance bactérienne aux médicaments</term><term>Peptides antimicrobiens cationiques</term><term>Pseudomonas aeruginosa</term><term>Tryptophane</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We previously reported a series of de novo engineered cationic antibiotic peptides (eCAPs) consisting exclusively of arginine and tryptophan (WR) that display potent activity against diverse multidrug-resistant (MDR) bacterial strains. In this study, we sought to examine the influence of arginine compared to lysine on antibacterial properties by direct comparison of the WR peptides (8-18 residues) with a parallel series of engineered peptides containing only lysine and tryptophan. WR and WK series were compared for antibacterial activity by bacterial killing and growth inhibition assays and for mechanism of peptide-bacteria interactions by surface plasmon resonance and flow cytometry. Mammalian cytotoxicity was also assessed by flow cytometry, haemolytic and tetrazolium-based assays. The shortest arginine-containing peptides (8 and 10 mers) displayed a statistically significant increase in activity compared to the analogous lysine-containing peptides. The WR and WK peptides achieved maximum antibacterial activity at the 12-mer peptide (WK12 or WR12). Further examination of antibacterial mechanisms of the optimally active 12-mer peptides using surface plasmon resonance and flow cytometry demonstrates stronger interactions with Pseudomonasaeruginosa, greater membrane permeabilizing activity, and lower inhibitory effects of divalent cations on activity and membrane permeabilization properties of WR12 compared to WK12 (P < 0.05). Importantly, WK12 and WR12 displayed similar negligible haemolytic and cytotoxic effects at peptide concentrations up to ten times the MIC or 20 times the minimum bactericidal concentration. Thus, arginine, compared to lysine, can indeed yield enhanced antibacterial activity to minimize the required length to achieve functional antimicrobial peptides. </div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Pennsylvanie</li></region></list><tree><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Deslouches, Berthony" sort="Deslouches, Berthony" uniqKey="Deslouches B" first="Berthony" last="Deslouches">Berthony Deslouches</name></region><name sortKey="Craigo, Jodi K" sort="Craigo, Jodi K" uniqKey="Craigo J" first="Jodi K" last="Craigo">Jodi K. Craigo</name><name sortKey="Hasek, Mary L" sort="Hasek, Mary L" uniqKey="Hasek M" first="Mary L" last="Hasek">Mary L. Hasek</name><name sortKey="Montelaro, Ronald C" sort="Montelaro, Ronald C" uniqKey="Montelaro R" first="Ronald C" last="Montelaro">Ronald C. Montelaro</name><name sortKey="Steckbeck, Jonathan D" sort="Steckbeck, Jonathan D" uniqKey="Steckbeck J" first="Jonathan D" last="Steckbeck">Jonathan D. Steckbeck</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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