Ion channel structure. Final technical report, April 1, 1993--March 31, 1997
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.
- Research Organization:
- Rice Univ., Houston, TX (United States)
- Sponsoring Organization:
- USDOE Office of Energy Research, Washington, DC (United States)
- DOE Contract Number:
- FG03-93ER61565
- OSTI ID:
- 570141
- Report Number(s):
- DOE/ER/61565-T1; ON: DE98002741; TRN: 98:001134
- Resource Relation:
- Other Information: PBD: [1998]
- Country of Publication:
- United States
- Language:
- English
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