Protein Adsorption and Reorganization on Nanoparticles Probed by the Coffee-Ring Effect: Application to Single Point Mutation Detection

Stéphanie Devineau 1 Manos Anyfantakis 1 Laurent Marichal 2 Laurent Kiger 3 Mathieu Morel 1 Sergii Rudiuk 1 Damien Baigl 1
1 PASTEUR - Processus d'Activation Sélective par Transfert d'Energie Uni-électronique ou Radiatif (UMR 8640)
2 LIONS - Laboratoire Interdisciplinaire sur l'Organisation Nanométrique et Supramoléculaire
NIMBE UMR 3685 - Nanosciences et Innovation pour les Matériaux, la Biomédecine et l'Energie (ex SIS2M)
3 IMRB - Institut Mondor de Recherche Biomédicale
Abstract : The coffee-ring effect denotes the accumulation of particles at the edge of an evaporating sessile drop pinned on a substrate. Because it can be detected by simple visual inspection, this ubiquitous phenomenon can be envisioned as a robust and cost-effective diagnostic tool. Toward this direction, here we systematically analyze the deposit morphology of drying drops containing polystyrene particles of different surface properties with various proteins (bovine serum albumin (BSA) and different forms of hemoglobin). We show that deposit patterns reveal information on both the adsorption of proteins onto particles and their reorganization following adsorption. By combining pattern analysis with adsorption isotherm and zeta potential measurements, we show that the suppression of the coffee-ring effect and the formation of a disk-shaped pattern is primarily associated with particle neutralization by protein adsorption. However, our findings also suggest that protein reorganization following adsorption can dramatically invert this tendency. Exposure of hydrophobic (respectively charged) residues can lead to disk (respectively ring) deposit morphologies independently of the global particle charge. Surface tension measurements and microscopic observations of the evaporating drops show that the determinant factor of the deposit morphology is the accumulation of particles at the liquid/ gas interface during evaporation. This general behavior opens the possibility to probe protein adsorption and reorganization on particles by the analysis of the deposit patterns, the formation of a disk being the robust signature of particles rendered hydrophobic by protein adsorption. We show that this method is sensitive enough to detect a single point mutation in a protein, as demonstrated here by the distinct patterns formed by human native hemoglobin h-HbA and its mutant form h-HbS, which is responsible for sickle cell anemia.
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Journal articles
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https://hal-cea.archives-ouvertes.fr/cea-01380676
Contributor : Serge Palacin <>
Submitted on : Thursday, October 13, 2016 - 12:22:49 PM
Last modification on : Friday, October 4, 2019 - 1:39:59 AM

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CEA | CNRS | UPMC | ENS-PARIS | IMRB | DSM-IRAMIS | UPEC-UPEM | PASTEUR_UMR8640 | PUBNIMBE | IRAMIS-NIMBE | CEA-UPSAY | INC-CNRS | PSL | UNIV-PARIS-SACLAY | CEA-DRF | SORBONNE-UNIVERSITE | SU-SCIENCES | UPEC

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Stéphanie Devineau, Manos Anyfantakis, Laurent Marichal, Laurent Kiger, Mathieu Morel, et al.. Protein Adsorption and Reorganization on Nanoparticles Probed by the Coffee-Ring Effect: Application to Single Point Mutation Detection. Journal of the American Chemical Society, American Chemical Society, 2016, 138, pp.11623 - 11632. ⟨10.1021/jacs.6b04833⟩. ⟨cea-01380676⟩

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