Novel atrazine-binding biomimetics inspired to the D1 protein from the photosystem II of Chlamydomonas reinhardtii

Giampaolo Barone, Fabrizio Lo Celso, Emanuela Gatto, Maria Moccia, Amina Antonacci, Fabrizio Lo Celso, Fabrizio Lo Celso, Jörg Grunenberg, Maria Teresa Giardi, Pietro Calandra, Viviana Scognamiglio

Risultato della ricerca: Articlepeer review

4 Citazioni (Scopus)

Abstract

Biomimetic design represents an emerging field for improving knowledge of natural molecules, as well as to project novel artificial tools with specific functions for biosensing. Effective strategies have been exploited to design artificial bioreceptors, taking inspiration from complex supramolecular assemblies. Among them, size-minimization strategy sounds promising to provide bioreceptors with tuned sensitivity, stability, and selectivity, through the ad hoc manipulation of chemical species at the molecular scale. Herein, a novel biomimetic peptide enabling herbicide binding was designed bioinspired to the D1 protein of the Photosystem II of the green alga Chlamydomonas reinhardtii. The D1 protein portion corresponding to the QB plastoquinone binding niche is capable of interacting with photosynthetic herbicides. A 50-mer peptide in the region of D1 protein from the residue 211 to 280 was designed in silico, and molecular dynamic simulations were performed alone and in complex with atrazine. An equilibrated structure was obtained with a stable pocked for atrazine binding by three H-bonds with SER222, ASN247, and HIS272 residues. Computational data were confirmed by fluorescence spectroscopy and circular dichroism on the peptide obtained by automated synthesis. Atrazine binding at nanomolar concentrations was followed by fluorescence spectroscopy, highlighting peptide suitability for optical sensing of herbicides at safety limits.
Lingua originaleEnglish
pagine (da-a)817-823
Numero di pagine7
RivistaInternational Journal of Biological Macromolecules
Volume163
Stato di pubblicazionePublished - 2020

All Science Journal Classification (ASJC) codes

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