期刊
CHEMISTRY & BIOLOGY
卷 17, 期 9, 页码 970-980出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2010.07.007
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资金
- Natural Sciences and Engineering Research Council of Canada
- Canada Foundation for Innovation
- Foundation for the National Institutes of Health
- Canadian Institutes for Health Research through Global Health Initiative
- Genome BC
- Canada Research Chair
- Canadian Cystic Fibrosis Foundation
The structure and function of the synthetic innate defense regulator peptide 1018 was investigated. This 12 residue synthetic peptide derived by substantial modification of the bovine cathelicidin bactenecin has enhanced innate immune regulatory and moderate direct antibacterial activities. The solution state NMR structure of 1018 in zwitterionic dodecyl phosphocholine (DPC) micelles indicated an alpha-helical conformation, while secondary structures, based on circular dichroism measurements, in anionic sodium dodecyl sulfate (SDS) and phospholipid vesicles (POPC/PG in a 1:1 molar ratio) and simulations revealed that 1018 can adopt a variety of folds, tailored to its different functions. The structural data are discussed in light of the ability of 1018 to potently induce chemokine responses, suppress the LPS-induced TNF-alpha response, and directly kill both Gram-positive and Gram-negative bacteria.
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