Linked Life Data

20438783

Source:http://linkedlifedata.com/resource/pubmed/id/20438783

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2010-7-16
pubmed:abstractText
Multimeric peptides offer several advantages with respect to their monomeric counterparts, as increased activity and greater stability to peptidases and proteases. SB041 is a novel antimicrobial peptide with dendrimeric structure; it is a tetramer of pyrEKKIRVRLSA linked by a lysine core, with an amino valeric acid chain. Here, we report on its synthesis, NMR characterization, antimicrobial activity, and LPS-interaction properties. The peptide was especially active against Gram-negative strains, with a potency comparable (on molar basis) to that of lipopeptides colistin and polymixin B, but it also displayed some activity against selected Gram-positive strains. Following these indications, we investigated the efficacy of SB041 in binding Escherichia coli and Pseudomonas aeruginosa LPS in vitro and counteracting its biological effects in RAW-Blue cells, derived from RAW 264.7 macrophages. SB041 strongly bound purified LPS, especially that of E. coli, as proved by fluorescent displacement assay, and readily penetrated into LPS monolayers. However, the killing activity of SB041 against E. coli was not inhibited by increasing concentrations of LPS added to the medium. Checking the SB041 effect on LPS-induced activation of pattern recognition receptors (PRRs) in Raw-Blue cells revealed that while the peptide gave a statistically significant decrease in PRRs stimulation when RAW-Blue cells were challenged with P. aeruginosa LPS, the same was not seen when E. coli LPS was used to activate innate immune defense-like responses. Thus, as previously seen for other antimicrobial peptides, also for SB041 binding to LPS did not translate necessarily into LPS-neutralizing activity, suggesting that SB041-LPS interactions must be of complex nature.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1873-5169
pubmed:author
pubmed:copyrightInfo
Copyright 2010 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1459-67
pubmed:meshHeading
pubmed-meshheading:20438783-Animals, pubmed-meshheading:20438783-Anti-Infective Agents, pubmed-meshheading:20438783-Antimicrobial Cationic Peptides, pubmed-meshheading:20438783-Candida, pubmed-meshheading:20438783-Cell Line, pubmed-meshheading:20438783-Dendrimers, pubmed-meshheading:20438783-Dose-Response Relationship, Drug, pubmed-meshheading:20438783-Dose-Response Relationship, Immunologic, pubmed-meshheading:20438783-Drug Design, pubmed-meshheading:20438783-Escherichia coli, pubmed-meshheading:20438783-Gram-Negative Bacteria, pubmed-meshheading:20438783-Gram-Positive Bacteria, pubmed-meshheading:20438783-Immunity, Innate, pubmed-meshheading:20438783-Kinetics, pubmed-meshheading:20438783-Lipopolysaccharides, pubmed-meshheading:20438783-Macrophages, pubmed-meshheading:20438783-Mice, pubmed-meshheading:20438783-Molecular Mimicry, pubmed-meshheading:20438783-Nuclear Magnetic Resonance, Biomolecular, pubmed-meshheading:20438783-Peptides, pubmed-meshheading:20438783-Protein Conformation, pubmed-meshheading:20438783-Pseudomonas aeruginosa, pubmed-meshheading:20438783-Receptors, Pattern Recognition
pubmed:year
2010
pubmed:articleTitle
Synthesis, characterization, antimicrobial activity and LPS-interaction properties of SB041, a novel dendrimeric peptide with antimicrobial properties.
pubmed:affiliation
Research & Development Unit, Spider Biotech S.r.l., I-10010 Colleretto Giacosa (TO), Italy.
pubmed:publicationType
Journal Article