Interaction between glyphosate pesticide and amphiphilic peptides for colorimetric analysis
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A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
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Date
2022-07-28
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Language
en
Pages
8
3592-3599
3592-3599
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Nanoscale Advances, Volume 4, issue 17
Abstract
The large-scale use of glyphosate pesticides in food production has attracted attention due to environmental damage and toxicity risks. Several regulatory authorities have established safe limits or concentrations of these pesticides in water and various food products consumed daily. The irreversible inhibition of acetylcholinesterase (AChE) activity is one of the strategies used for pesticide detection. Herein, we found that lipopeptide sequences can act as biomimetic microenvironments of AChE, showing higher catalytic activities than natural enzymes in an aqueous solution, based on IC50 values. These biomolecules contain in the hydrophilic part the amino acids l-proline (P), l-arginine (R), l-tryptophan (W), and l-glycine (G), covalently linked to a hydrophobic part formed by one or two long aliphatic chains. The obtained materials are referred to as compounds 1 and 2, respectively. According to fluorescence assays, 2 is more hydrophobic than 1. The circular dichroism (CD) data present a significant difference in the molar ellipticity values, likely related to distinct conformations assumed by the proline residue in the lipopeptide supramolecular structure in solution. The morphological aspect was further characterized using small-angle X-ray scattering (SAXS) and cryogenic transmission electron microscopy (cryo-TEM), which showed that compounds 1 and 2 self-assembly into cylindrical and planar core-shell structures, respectively. The mimetic AchE behaviour of lipopeptides was confirmed by Ellman's hydrolysis reaction, where the proline residue in the peptides act as a nucleophilic scavenger of organophosphate pesticides. Moreover, the isothermal titration calorimetry (ITC) experiments revealed that host-guest interactions in both systems were dominated by enthalpically-driven thermodynamics. UV-vis kinetic experiments were performed to assess the inhibition of the lipopeptide catalytic activity and the IC50 values were obtained, and we found that the detection limit correlated with the increase in hydrophobicity of the lipopeptides, implying the micellization process is more favorable.Description
Funding Information: This work was supported by FAPESP (grant no. 2017/02317-2), CNPq (grant no. 304389/2019-6), and the National Institute of Science and Technology in Bioanalytics (FAPESP grant no. 2014/50867-3 and CNPq grant no. 465389/2014-7) grants. B. B. G. and P. L. O. F. acknowledge FAPESP fellowships (project numbers 2018/05888-3, 2020/02192-8, 2019/12301-1, and 2020/13204-7). We thank Diamond Light Source for the award of SAXS beamtime (ref. SM28659-2), Dr Katsuaki Inoue for running the measurements, and the ESRF for the award of SAXS beamtime (ref. MX-2345), and Dr Mark Tully for the measurements. We acknowledge access to the Chemical Analysis Facility at the University of Reading. Publisher Copyright: © 2022 RSC.
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Gerbelli, B B, Filho, P L O, Cortez, B, Sodré, P T, Coutinho-Neto, M D, Hamley, I W, Seitsonen, J & Alves, W A 2022, ' Interaction between glyphosate pesticide and amphiphilic peptides for colorimetric analysis ', Nanoscale Advances, vol. 4, no. 17, pp. 3592-3599 . https://doi.org/10.1039/d2na00345g