Comparative functional properties of engineered cationic antimicrobial peptides consisting exclusively of tryptophan and either lysine or arginine.
Identifieur interne : 001183 ( PubMed/Corpus ); précédent : 001182; suivant : 001184Comparative functional properties of engineered cationic antimicrobial peptides consisting exclusively of tryptophan and either lysine or arginine.
Auteurs : Berthony Deslouches ; Mary L. Hasek ; Jodi K. Craigo ; Jonathan D. Steckbeck ; Ronald C. MontelaroSource :
- Journal of medical microbiology [ 1473-5644 ] ; 2016.
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
Links to Exploration step
pubmed:27046192Le document en format XML
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Hasek</name><affiliation><nlm:affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</nlm:affiliation></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><nlm:affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Steckbeck, Jonathan D" sort="Steckbeck, Jonathan D" uniqKey="Steckbeck J" first="Jonathan D" last="Steckbeck">Jonathan D. Steckbeck</name><affiliation><nlm:affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Montelaro, Ronald C" sort="Montelaro, Ronald C" uniqKey="Montelaro R" first="Ronald C" last="Montelaro">Ronald C. 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Hasek</name><affiliation><nlm:affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</nlm:affiliation></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><nlm:affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Steckbeck, Jonathan D" sort="Steckbeck, Jonathan D" uniqKey="Steckbeck J" first="Jonathan D" last="Steckbeck">Jonathan D. Steckbeck</name><affiliation><nlm:affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Montelaro, Ronald C" sort="Montelaro, Ronald C" uniqKey="Montelaro R" first="Ronald C" last="Montelaro">Ronald C. Montelaro</name><affiliation><nlm:affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</nlm:affiliation></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="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" xml:lang="en"><term>Drug Resistance, Multiple, Bacterial</term><term>Humans</term><term>Protein Binding</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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27046192</PMID><DateCompleted><Year>2017</Year><Month>01</Month><Day>26</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1473-5644</ISSN><JournalIssue CitedMedium="Internet"><Volume>65</Volume><Issue>6</Issue><PubDate><Year>2016</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Journal of medical microbiology</Title><ISOAbbreviation>J. Med. Microbiol.</ISOAbbreviation></Journal><ArticleTitle>Comparative functional properties of engineered cationic antimicrobial peptides consisting exclusively of tryptophan and either lysine or arginine.</ArticleTitle><Pagination><MedlinePgn>554-565</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1099/jmm.0.000258</ELocationID><Abstract><AbstractText>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. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Deslouches</LastName><ForeName>Berthony</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hasek</LastName><ForeName>Mary L</ForeName><Initials>ML</Initials><AffiliationInfo><Affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Craigo</LastName><ForeName>Jodi K</ForeName><Initials>JK</Initials><AffiliationInfo><Affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Steckbeck</LastName><ForeName>Jonathan D</ForeName><Initials>JD</Initials><AffiliationInfo><Affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Montelaro</LastName><ForeName>Ronald C</ForeName><Initials>RC</Initials><AffiliationInfo><Affiliation>Center for Vaccine Research and Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P30 DK072506</GrantID><Acronym>DK</Acronym><Agency>NIDDK NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>04</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Med Microbiol</MedlineTA><NlmUniqueID>0224131</NlmUniqueID><ISSNLinking>0022-2615</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D023181">Antimicrobial Cationic Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>8DUH1N11BX</RegistryNumber><NameOfSubstance UI="D014364">Tryptophan</NameOfSubstance></Chemical><Chemical><RegistryNumber>94ZLA3W45F</RegistryNumber><NameOfSubstance UI="D001120">Arginine</NameOfSubstance></Chemical><Chemical><RegistryNumber>K3Z4F929H6</RegistryNumber><NameOfSubstance 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| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a MersV1
| This area was generated with Dilib version V0.6.33. |  |