Ion channel structure. Final technical report, April 1, 1993--March 31, 1997

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During the past decade, endogenous antimicrobial peptides have become recognized as important, ubiquitous, and ancient contributors to the innate mechanisms which permit animals (including humans), and plants to resist infection. Most of these host defense peptides are small (18-35 amino acids), amphipathic and possess either an {alpha}-helical or cystine-stabilized {beta}-sheet structure. These peptides are probably too small for enzymatic function and, so far, no specific receptors have been found. All evidence indicates that their target of action is the lipid matrix of the bacterial cytoplasmic membranes. This project aimed at clarifying the mechanism of peptide-membrane interactions, in particular the pore ... continued below

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7 p.

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Creator: Unknown. February 1, 1998.

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Description

During the past decade, endogenous antimicrobial peptides have become recognized as important, ubiquitous, and ancient contributors to the innate mechanisms which permit animals (including humans), and plants to resist infection. Most of these host defense peptides are small (18-35 amino acids), amphipathic and possess either an {alpha}-helical or cystine-stabilized {beta}-sheet structure. These peptides are probably too small for enzymatic function and, so far, no specific receptors have been found. All evidence indicates that their target of action is the lipid matrix of the bacterial cytoplasmic membranes. This project aimed at clarifying the mechanism of peptide-membrane interactions, in particular the pore formation by the peptides which appear to be the mode of action of these antimicrobials. Tremendous progress was made during the project period. We summarize our findings in the following report.

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7 p.

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OSTI as DE98002741

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  • Other Information: PBD: [1998]

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  • Other: DE98002741
  • Report No.: DOE/ER/61565--T1
  • Grant Number: FG03-93ER61565
  • DOI: 10.2172/570141 | External Link
  • Office of Scientific & Technical Information Report Number: 570141
  • Archival Resource Key: ark:/67531/metadc691155

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Office of Scientific & Technical Information Technical Reports

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  • February 1, 1998

Added to The UNT Digital Library

  • Aug. 14, 2015, 8:43 a.m.

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  • Nov. 6, 2015, 3:23 p.m.

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Ion channel structure. Final technical report, April 1, 1993--March 31, 1997, report, February 1, 1998; United States. (digital.library.unt.edu/ark:/67531/metadc691155/: accessed December 15, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.