A family of kassinatuerin-2 related peptides from the skin secretion of the African hyperoliid frog, Kassina maculata.
Identifieur interne : 002016 ( PubMed/Corpus ); précédent : 002015; suivant : 002017A family of kassinatuerin-2 related peptides from the skin secretion of the African hyperoliid frog, Kassina maculata.
Auteurs : Lei Wang ; Mei Zhou ; Stephanie Mcgrath ; Tianbao Chen ; Sean P. Gorman ; Brian Walker ; Chris ShawSource :
- Peptides [ 1873-5169 ] ; 2009.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amphibian Proteins (chemistry), Amphibian Proteins (isolation & purification), Amphibian Proteins (pharmacology), Animals, Anti-Infective Agents (pharmacology), Anura (metabolism), Base Sequence, Candida albicans (drug effects), Chromatography, High Pressure Liquid, Escherichia coli (drug effects), Hemolysis (drug effects), Microbial Sensitivity Tests, Molecular Sequence Data, Peptides (chemistry), Peptides (isolation & purification), Peptides (pharmacology), Sequence Alignment, Sequence Homology, Amino Acid, Skin (metabolism).
- MESH :
- chemical , chemistry : Amphibian Proteins, Peptides.
- chemical , isolation & purification : Amphibian Proteins, Peptides.
- chemical , pharmacology : Amphibian Proteins, Anti-Infective Agents, Peptides.
- drug effects : Candida albicans, Escherichia coli, Hemolysis.
- metabolism : Anura, Skin.
- Amino Acid Sequence, Animals, Base Sequence, Chromatography, High Pressure Liquid, Microbial Sensitivity Tests, Molecular Sequence Data, Sequence Alignment, Sequence Homology, Amino Acid.
Abstract
We describe the isolation and structural characterization of a family of antimicrobial peptides related to kassinatuerin-2, from the skin secretion of the African hyperoliid frog, Kassina maculata. All four peptides, designated kassinatuerin-2Ma through Md, are C-terminally-amidated 20-mers with the consensus sequence - FX(1)GAIAAALPHVIX(2)AIKNAL - where X(1)=L/F/V/I and X2=S/N. All four peptides are encoded by precursors of 69 amino acids. Synthetic replicates of all kassinatuerin-2 related peptides displayed a potent inhibitory activity against Staphylococcus aureus with a minimal inhibitory concentration of 16microM, at which concentration, however, they effected 18% haemolysis of horse erythrocytes after 2h. Despite obvious membranolytic properties, all peptides were ineffective at inhibiting the growth of Escherichia coli at concentrations up to 200microM and were relatively ineffective against Candida albicans (MIC 120microM). The kassinatuerin-2 related peptides of K. maculata skin secretion thus possess a discrete antimicrobial and weak haemolytic activity in contrast to the prototype kassinatuerin-2 from the skin secretion of Kassina senegalensis.
DOI: 10.1016/j.peptides.2009.04.021
PubMed: 19427345
Links to Exploration step
pubmed:19427345Le document en format XML
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Gorman</name></author><author><name sortKey="Walker, Brian" sort="Walker, Brian" uniqKey="Walker B" first="Brian" last="Walker">Brian Walker</name></author><author><name sortKey="Shaw, Chris" sort="Shaw, Chris" uniqKey="Shaw C" first="Chris" last="Shaw">Chris Shaw</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19427345</idno><idno type="pmid">19427345</idno><idno type="doi">10.1016/j.peptides.2009.04.021</idno><idno type="wicri:Area/PubMed/Corpus">002016</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002016</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A family of kassinatuerin-2 related peptides from the skin secretion of the African hyperoliid frog, Kassina maculata.</title><author><name sortKey="Wang, Lei" sort="Wang, Lei" uniqKey="Wang L" first="Lei" last="Wang">Lei Wang</name><affiliation><nlm:affiliation>Molecular Therapeutics Research, School of Pharmacy, Queen's University, Lisburn Road, Belfast BT9 7BL, Northern Ireland, UK.</nlm:affiliation></affiliation></author><author><name sortKey="Zhou, Mei" sort="Zhou, Mei" uniqKey="Zhou M" first="Mei" last="Zhou">Mei Zhou</name></author><author><name sortKey="Mcgrath, Stephanie" sort="Mcgrath, Stephanie" uniqKey="Mcgrath S" first="Stephanie" last="Mcgrath">Stephanie Mcgrath</name></author><author><name sortKey="Chen, Tianbao" sort="Chen, Tianbao" uniqKey="Chen T" first="Tianbao" last="Chen">Tianbao Chen</name></author><author><name sortKey="Gorman, Sean P" sort="Gorman, Sean P" uniqKey="Gorman S" first="Sean P" last="Gorman">Sean P. Gorman</name></author><author><name sortKey="Walker, Brian" sort="Walker, Brian" uniqKey="Walker B" first="Brian" last="Walker">Brian Walker</name></author><author><name sortKey="Shaw, Chris" sort="Shaw, Chris" uniqKey="Shaw C" first="Chris" last="Shaw">Chris Shaw</name></author></analytic><series><title level="j">Peptides</title><idno type="eISSN">1873-5169</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Amphibian Proteins (chemistry)</term><term>Amphibian Proteins (isolation & purification)</term><term>Amphibian Proteins (pharmacology)</term><term>Animals</term><term>Anti-Infective Agents (pharmacology)</term><term>Anura (metabolism)</term><term>Base Sequence</term><term>Candida albicans (drug effects)</term><term>Chromatography, High Pressure Liquid</term><term>Escherichia coli (drug effects)</term><term>Hemolysis (drug effects)</term><term>Microbial Sensitivity Tests</term><term>Molecular Sequence Data</term><term>Peptides (chemistry)</term><term>Peptides (isolation & purification)</term><term>Peptides (pharmacology)</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term><term>Skin (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amphibian Proteins</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Amphibian Proteins</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Amphibian Proteins</term><term>Anti-Infective Agents</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Candida albicans</term><term>Escherichia coli</term><term>Hemolysis</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Anura</term><term>Skin</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Chromatography, High Pressure Liquid</term><term>Microbial Sensitivity Tests</term><term>Molecular Sequence Data</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We describe the isolation and structural characterization of a family of antimicrobial peptides related to kassinatuerin-2, from the skin secretion of the African hyperoliid frog, Kassina maculata. All four peptides, designated kassinatuerin-2Ma through Md, are C-terminally-amidated 20-mers with the consensus sequence - FX(1)GAIAAALPHVIX(2)AIKNAL - where X(1)=L/F/V/I and X2=S/N. All four peptides are encoded by precursors of 69 amino acids. Synthetic replicates of all kassinatuerin-2 related peptides displayed a potent inhibitory activity against Staphylococcus aureus with a minimal inhibitory concentration of 16microM, at which concentration, however, they effected 18% haemolysis of horse erythrocytes after 2h. Despite obvious membranolytic properties, all peptides were ineffective at inhibiting the growth of Escherichia coli at concentrations up to 200microM and were relatively ineffective against Candida albicans (MIC 120microM). The kassinatuerin-2 related peptides of K. maculata skin secretion thus possess a discrete antimicrobial and weak haemolytic activity in contrast to the prototype kassinatuerin-2 from the skin secretion of Kassina senegalensis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19427345</PMID><DateCompleted><Year>2009</Year><Month>10</Month><Day>08</Day></DateCompleted><DateRevised><Year>2009</Year><Month>07</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-5169</ISSN><JournalIssue CitedMedium="Internet"><Volume>30</Volume><Issue>8</Issue><PubDate><Year>2009</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Peptides</Title><ISOAbbreviation>Peptides</ISOAbbreviation></Journal><ArticleTitle>A family of kassinatuerin-2 related peptides from the skin secretion of the African hyperoliid frog, Kassina maculata.</ArticleTitle><Pagination><MedlinePgn>1428-33</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.peptides.2009.04.021</ELocationID><Abstract><AbstractText>We describe the isolation and structural characterization of a family of antimicrobial peptides related to kassinatuerin-2, from the skin secretion of the African hyperoliid frog, Kassina maculata. All four peptides, designated kassinatuerin-2Ma through Md, are C-terminally-amidated 20-mers with the consensus sequence - FX(1)GAIAAALPHVIX(2)AIKNAL - where X(1)=L/F/V/I and X2=S/N. All four peptides are encoded by precursors of 69 amino acids. Synthetic replicates of all kassinatuerin-2 related peptides displayed a potent inhibitory activity against Staphylococcus aureus with a minimal inhibitory concentration of 16microM, at which concentration, however, they effected 18% haemolysis of horse erythrocytes after 2h. Despite obvious membranolytic properties, all peptides were ineffective at inhibiting the growth of Escherichia coli at concentrations up to 200microM and were relatively ineffective against Candida albicans (MIC 120microM). The kassinatuerin-2 related peptides of K. maculata skin secretion thus possess a discrete antimicrobial and weak haemolytic activity in contrast to the prototype kassinatuerin-2 from the skin secretion of Kassina senegalensis.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Lei</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Molecular Therapeutics Research, School of Pharmacy, Queen's University, Lisburn Road, Belfast BT9 7BL, Northern Ireland, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhou</LastName><ForeName>Mei</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>McGrath</LastName><ForeName>Stephanie</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Tianbao</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Gorman</LastName><ForeName>Sean P</ForeName><Initials>SP</Initials></Author><Author ValidYN="Y"><LastName>Walker</LastName><ForeName>Brian</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Shaw</LastName><ForeName>Chris</ForeName><Initials>C</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>05</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Peptides</MedlineTA><NlmUniqueID>8008690</NlmUniqueID><ISSNLinking>0196-9781</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029845">Amphibian Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000890">Anti-Infective 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