Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

Oxidized phospholipids as potential molecular targets for antimicrobial peptides.

Oxidized phospholipids as potential molecular targets for antimicrobial peptides. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

  • Abstract Text of This Paper
  • Journal Published
  • MeSH Keywords of This Abstract
  • Chemicals and Substances Used in this Paper
  • Grants and Granting Agency of this Research
  • Database Accession Numbers Used in this Paper
  • Related Papers
  • Related Research Tags
  • Rate this Research Paper
  • Oxidized phospholipids as potential molecular targets for antimicrobial peptides. Abstract Text:

    The effects of oxidatively modified phospholipids on the association with model biomembranes of four antimicrobial peptides (AMPs), temporin B and L, indolicidin, and LL-37(F27W) were studied by Langmuir balance and fluorescence spectroscopy. In keeping with previous reports the negatively charged phospholipid phosphatidylglycerol (PG) enhanced the intercalation of all four peptides into lipid monolayers and liposomal bilayers under low ionic strength conditions. Interestingly, similar effect was observed for 1-palmitoyl-2-(9'-oxo-nonanoyl)-sn-glycero-3-phosphocholine (PoxnoPC), a zwitterionic oxidized phospholipid bearing an aldehyde function at the end of its truncated sn-2 acyl chain. Instead, the structurally similar 1-palmitoyl-2-azelaoyl-sn-glycero-3-phosphocholine (PazePC) containing a carboxylic moiety was less efficient in promoting the membrane association of these peptides. Physiological saline reduced the binding of the above peptides to membranes containing PG, whereas interactions with PoxnoPC were found to be insensitive to ionic strength. Notably, membrane intercalation of temporin L, the most surface active of the above peptides could be into PoxnoPC containing monolayers was strongly attenuated by methoxyamine, suggesting the importance of Schiff base formation between peptide amino groups and the lipid aldehyde function. PoxnoPC and similar aldehyde bearing oxidatively modified phospholipids could represent novel molecular targets for AMPs.

    Oxidized phospholipids as potential molecular targets for antimicrobial peptides. Publishing Authors By Initials

    For similar abstracts research abstracts see: abstracts research

    PUBMED ID PMID:

    MEDLINE DATE:

    Oxidized phospholipids as potential molecular targets for antimicrobial peptides. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Biochimica et biophysica acta

    VOLUME: 1778

    Page Numbers: 2041-50

    Journal Abbreviation: Biochim. Biophys. Acta

    ISSN: 0006-3002

    DAY: 8

    MONTH: 04

    YEAR: 2008

    Oxidized phospholipids as potential molecular targets for antimicrobial peptides. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 217513

    Oxidized phospholipids as potential molecular targets for antimicrobial peptides. Keywords Mesh Terms:

    KEYWORDS:

    MESH TERMS:

    Chemical & Substance for Abstract: Oxidized phospholipids as potential molecular targets for antimicrobial peptides. Information

    Substance Name:

    Registry Number:

    Grant and Affiliation Information for Oxidized phospholipids as potential molecular targets for antimicrobial peptides.

    AFFILIATION: Helsinki Biophysics and Biomembrane Group, Institute of Biomedicine/Medical Biochemistry, P.O. Box 63 (Haartmaninkatu 8), FIN-00014 University of Helsinki, Helsinki, Finland.

    Country: Netherlands

    Netherlands Research PublicationNetherlands Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: Biochim Biophys Acta

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Oxidized phospholipids as potential molecular targets for antimicrobial peptides Related Publications

     

    Molecular Station USER Menu

    Welcome to Molecular Station!

    You have to register before you can post on our forums or use our advanced features. Register Now! Its Free and Fast!

    Already registered? Login now below.

    User Name:

    Password:

    Already registered and Forgot your password? Click below to recover it.

    Recover Lost Password

    Join now - it's fast and free!

    Molecular Station is THE largest network of researchers, scientists and science lovers anywhere!

    Research Terms of Usage and Disclaimer
    Home
    Features

    Protocols

    DNA Forum

    Science Forum

    DNA Forum
    Biology Forum

    Science News


    [CaRP] XML error: Invalid document end at line 2

    For more click here:Science News