Structure and membrane interactions of the antibiotic peptide dermadistinctin k by solution and oriented 15N and 31P solid-state NMR spectroscopy
Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy
The peptide was synthesized by solid-phase synthesis using fmoc chemistry. The peptide is an antimicrobial peptide that is naturally found from the skin secretion of phyllomedusa distincta, a frog species found in brazilian forests.
NOE intensities were converted into semi-quantitative distances restrains. The upper limits of the distances thus obtained were 2.8, 3.4 and 5.0A; (for strong, medium, and weak NOEs, respectively). Structure calculations were performed using the Xplor-NIH software, version 2.17.0 . Starting with the extended structure, 500 structures were generated using a simulated annealing protocol. This was followed by 20000 steps of simulated annealing at 1000 K and a subsequent decrease in tempera ure in 15000 steps in the first slow-cool annealing stage.
2.0mM dermadistinctin k; trifluoroethanol; H2O 60%, D2O 40%
Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
Schwieters, Kuszewski, Tjandra and Clore
Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Th
ALPHA HELIX, AMPHIPATHIC CHARACTER, C-TERMINAL CARBOXYAMIDATION, MEMBRANE PEPTIDE, Amphibian defense peptide, Antibiotic, Antimicrobial, Secreted, ANTIMICROBIAL PROTEIN