| Title | Structural Studies of a Peptide with Immune Modulating and Direct Antimicrobial Activity. |
| Publication Type | Journal Article |
| Year of Publication | 2010 |
| Authors | Wieczorek, M, Jenssen, H, Kindrachuk, J, Scott, WRP, Elliott, M, Hilpert, K, Cheng, JTJ, Hancock, REW, Straus, SK |
| Journal | Chemistry & Biology (Cambridge, MA, United States) |
| Volume | 17 |
| Pagination | 970 - 980 |
| Date Published | 2010/// |
| ISBN Number | 1074-5521 |
| Keywords | IDR 1018 peptide alpha helix antimicrobial activity immunomodulation |
| Abstract | Summary: 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 soln. state NMR structure of 1018 in zwitterionic dodecyl phosphocholine (DPC) micelles indicated an α-helical conformation, while secondary structures, based on CD 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-α response, and directly kill both Gram-pos. and Gram-neg. bacteria. [on SciFinder(R)] |
