Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes |
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Affiliation: | 1. Separtment of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA;2. Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA;3. Department of Medicine, University of California, Los Angeles, CA 90095, USA |
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Abstract: | Background: The protegrins are a family of arginine- and cysteine-rich cationic peptides found in porcine leukocytes that exhibit a broad range of antimicrobial and antiviral activities. They are composed of 16–18 amino-acid residues including four cysteines, which form two disulfide linkages. To begin to understand the mechanism of action of these peptides, we set out to determine the structure of protegrin-1 (PG-1).Results: We used two-dimensional homonuclear nuclear magnetic resonance spectroscopy to study the conformation of both natural and synthetic PG-1 under several conditions. A refined three-dimensional structure of synthetic PG-1 is presented.Conclusions: Both synthetic and natural protegrin-1 form a well-defined structure in solution composed primarily of a two-stranded antiparallel β sheet, with strands connected by a β turn. The structure of PG-1 suggests ways in which the peptide may interact with itself or other molecules to form the membrane pores and the large membrane-associated assemblages observed in protegrin-treated, gram-negative bacteria. |
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