Structure-function relationships in novel peptide dodecamerswith broad-spectrum bactericidal and endotoxin-neutralizing activities.
Identifieur interne : 002433 ( PubMed/Checkpoint ); précédent : 002432; suivant : 002434Structure-function relationships in novel peptide dodecamerswith broad-spectrum bactericidal and endotoxin-neutralizing activities.
Auteurs : K H Mayo [États-Unis] ; J. Haseman ; H C Young ; J W MayoSource :
- The Biochemical journal [ 0264-6021 ] ; 2000.
Descripteurs français
- KwdFr :
- MESH :
- antagonistes et inhibiteurs : Endotoxines.
- pharmacologie : Antibactériens.
- Dichroïsme circulaire, Données de séquences moléculaires, Humains, Hémolyse, Peptides, Pseudomonas aeruginosa, Relation structure-activité, Spectroscopie par résonance magnétique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Anti-Bacterial Agents (pharmacology), Circular Dichroism, Endotoxins (antagonists & inhibitors), Hemolysis (drug effects), Humans, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Peptides (chemistry), Pseudomonas aeruginosa (drug effects), Structure-Activity Relationship.
- MESH :
- chemical , antagonists & inhibitors : Endotoxins.
- chemical , chemistry : Peptides.
- chemical , pharmacology : Anti-Bacterial Agents.
- drug effects : Hemolysis, Pseudomonas aeruginosa.
- Amino Acid Sequence, Circular Dichroism, Humans, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Structure-Activity Relationship.
Abstract
A series of designed peptide 33-mers (betapep peptides) areknown to be bactericidal [Mayo, Haseman, Ilyina and Gray (1998)Biochim. Biophys. Acta 1425, 81-92]. Here dodecapeptides (SC-1-SC-8), which 'walk through' the sequence ofbetapep-25, were investigated for their ability to kill Gram-negativeand -positive bacteria and to neutralize endotoxin. SC-4 (KLFKRHLKWKI I-NH(2); the -NH(2) at the right of each sequenceindicates amidation of the C-terminal carboxylate group) is the mosteffective, more so than betapep-25, at killing Gram-negative bacteriawith nanomolar LD(50) values. Against Gram-positive bacteria,SC-4 also shows good activity with submicromolar LD(50)values. Leakage studies indicate rapid bacterial membrane permeability,with t(1/2) valuesof 10-15 min. SC-4 in the micromolar range also effectivelyneutralizes endotoxin and is not haemolytic below 10(-4)M. For all SC peptides, CD and NMR data indicate the presence of both 3(10)- and alpha-helix. For SC-4, nuclear-Overhauser-effect-based computational modelling yields an amphipathic helix with K1, K4,R5, and K8 arrayed on the same face (K is lysine, R is arginine). Activity differences among SC peptides and single-site variants of SC-4allow some structure-function relationships to be deduced. Relative to other known bactericidal peptides in the linear peptide,helix-forming category, SC-4 is the most potent broad-spectrumantibacterial identified to date. The present study contributes to thedevelopment of agents involved in combating the ever-recurring problemof drug-resistant micro-organisms.
DOI: 10.1042/bj3490717
PubMed: 10903132
Affiliations:
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Haseman</name></author><author><name sortKey="Young, H C" sort="Young, H C" uniqKey="Young H" first="H C" last="Young">H C Young</name></author><author><name sortKey="Mayo, J W" sort="Mayo, J W" uniqKey="Mayo J" first="J W" last="Mayo">J W Mayo</name></author></analytic><series><title level="j">The Biochemical journal</title><idno type="ISSN">0264-6021</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Anti-Bacterial Agents (pharmacology)</term><term>Circular Dichroism</term><term>Endotoxins (antagonists & inhibitors)</term><term>Hemolysis (drug effects)</term><term>Humans</term><term>Magnetic Resonance Spectroscopy</term><term>Molecular Sequence Data</term><term>Peptides (chemistry)</term><term>Pseudomonas aeruginosa (drug effects)</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antibactériens (pharmacologie)</term><term>Dichroïsme circulaire</term><term>Données de séquences moléculaires</term><term>Endotoxines (antagonistes et inhibiteurs)</term><term>Humains</term><term>Hémolyse ()</term><term>Peptides ()</term><term>Pseudomonas aeruginosa ()</term><term>Relation structure-activité</term><term>Spectroscopie par résonance magnétique</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Endotoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Anti-Bacterial Agents</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Endotoxines</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Hemolysis</term><term>Pseudomonas aeruginosa</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antibactériens</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Circular Dichroism</term><term>Humans</term><term>Magnetic Resonance Spectroscopy</term><term>Molecular Sequence Data</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dichroïsme circulaire</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Hémolyse</term><term>Peptides</term><term>Pseudomonas aeruginosa</term><term>Relation structure-activité</term><term>Spectroscopie par résonance magnétique</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A series of designed peptide 33-mers (betapep peptides) areknown to be bactericidal [Mayo, Haseman, Ilyina and Gray (1998)Biochim. Biophys. Acta 1425, 81-92]. Here dodecapeptides (SC-1-SC-8), which 'walk through' the sequence ofbetapep-25, were investigated for their ability to kill Gram-negativeand -positive bacteria and to neutralize endotoxin. SC-4 (KLFKRHLKWKI I-NH(2); the -NH(2) at the right of each sequenceindicates amidation of the C-terminal carboxylate group) is the mosteffective, more so than betapep-25, at killing Gram-negative bacteriawith nanomolar LD(50) values. Against Gram-positive bacteria,SC-4 also shows good activity with submicromolar LD(50)values. Leakage studies indicate rapid bacterial membrane permeability,with t(1/2) valuesof 10-15 min. SC-4 in the micromolar range also effectivelyneutralizes endotoxin and is not haemolytic below 10(-4)M. For all SC peptides, CD and NMR data indicate the presence of both 3(10)- and alpha-helix. For SC-4, nuclear-Overhauser-effect-based computational modelling yields an amphipathic helix with K1, K4,R5, and K8 arrayed on the same face (K is lysine, R is arginine). Activity differences among SC peptides and single-site variants of SC-4allow some structure-function relationships to be deduced. Relative to other known bactericidal peptides in the linear peptide,helix-forming category, SC-4 is the most potent broad-spectrumantibacterial identified to date. The present study contributes to thedevelopment of agents involved in combating the ever-recurring problemof drug-resistant micro-organisms.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10903132</PMID><DateCompleted><Year>2001</Year><Month>01</Month><Day>18</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0264-6021</ISSN><JournalIssue CitedMedium="Print"><Volume>349 Pt 3</Volume><PubDate><Year>2000</Year><Month>Aug</Month><Day>01</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem. J.</ISOAbbreviation></Journal><ArticleTitle>Structure-function relationships in novel peptide dodecamerswith broad-spectrum bactericidal and endotoxin-neutralizing activities.</ArticleTitle><Pagination><MedlinePgn>717-28</MedlinePgn></Pagination><Abstract><AbstractText>A series of designed peptide 33-mers (betapep peptides) areknown to be bactericidal [Mayo, Haseman, Ilyina and Gray (1998)Biochim. Biophys. Acta 1425, 81-92]. Here dodecapeptides (SC-1-SC-8), which 'walk through' the sequence ofbetapep-25, were investigated for their ability to kill Gram-negativeand -positive bacteria and to neutralize endotoxin. SC-4 (KLFKRHLKWKI I-NH(2); the -NH(2) at the right of each sequenceindicates amidation of the C-terminal carboxylate group) is the mosteffective, more so than betapep-25, at killing Gram-negative bacteriawith nanomolar LD(50) values. Against Gram-positive bacteria,SC-4 also shows good activity with submicromolar LD(50)values. Leakage studies indicate rapid bacterial membrane permeability,with t(1/2) valuesof 10-15 min. SC-4 in the micromolar range also effectivelyneutralizes endotoxin and is not haemolytic below 10(-4)M. For all SC peptides, CD and NMR data indicate the presence of both 3(10)- and alpha-helix. For SC-4, nuclear-Overhauser-effect-based computational modelling yields an amphipathic helix with K1, K4,R5, and K8 arrayed on the same face (K is lysine, R is arginine). Activity differences among SC peptides and single-site variants of SC-4allow some structure-function relationships to be deduced. Relative to other known bactericidal peptides in the linear peptide,helix-forming category, SC-4 is the most potent broad-spectrumantibacterial identified to date. The present study contributes to thedevelopment of agents involved in combating the ever-recurring problemof drug-resistant micro-organisms.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mayo</LastName><ForeName>K H</ForeName><Initials>KH</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Molecular Biology and Biophysics and The Biomedical Engineering Center, University of Minnesota Health Science Center, 6-155 Jackson Hall, 321 Church Street, Minneapolis, MN 55455, USA. mayox001@maroon.tc.umn.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Haseman</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Young</LastName><ForeName>H C</ForeName><Initials>HC</Initials></Author><Author ValidYN="Y"><LastName>Mayo</LastName><ForeName>J W</ForeName><Initials>JW</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal 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Haseman</name><name sortKey="Mayo, J W" sort="Mayo, J W" uniqKey="Mayo J" first="J W" last="Mayo">J W Mayo</name><name sortKey="Young, H C" sort="Young, H C" uniqKey="Young H" first="H C" last="Young">H C Young</name></noCountry><country name="États-Unis"><region name="Minnesota"><name sortKey="Mayo, K H" sort="Mayo, K H" uniqKey="Mayo K" first="K H" last="Mayo">K H Mayo</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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