期刊
JOURNAL OF COLLOID AND INTERFACE SCIENCE
卷 530, 期 -, 页码 328-337出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jcis.2018.06.065
关键词
Organophosphates; beta-sheet; beta-hairpin; Catalytic triad; Thioflavin T; Circular dichroism; Surface enhanced Raman spectroscopy
资金
- IDF medical corps grant [1542-2015]
- Israel Ministry of Agriculture
- Ministry of Science of China
- Ministry of Science of Israel
Organophosphate compounds that are used as pesticides affect the nervous system by binding irreversibly to the active site of the enzyme acetylcholine esterase (AChE) and disrupting neuro-signaling nerve cells. In this study we characterized adsorption of paraoxon to a set of designed peptides that present different arrangements of the three amino acids of the AChE catalytic site: histidine, glutamic-acid and serine. The peptides set included two beta-strands with no net charge and three beta-hairpins that differ in their net charge. Circular dichroism, Thioflavin T assays and TEM images provided only qualitative insights on paraoxon binding to the different peptides. Paraoxon binding to the different peptides was measured with dialysis membrane tubes filled with the peptide solutions and suspended in a reservoir of paraoxon solution. Among all the tested peptides, the single strand peptide, denoted ssESH exhibited at 100 mu M in random conformation prefibrillar state, the maximum paraoxon adsorption, with a binding mol ratio of one paraoxon per two peptides and an estimated equilibrium binding constant 5 * 10(4) M-1 The three beta-hairpin peptides demonstrated that a net negative charge is unfavorable for paraoxon adsorption. Surface enhanced Raman spectroscopy measurements with ssESH enabled the detection of nanomolar adsorbed concentrations of paraoxon. (C) 2018 Published by Elsevier Inc.
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