title: Protein Adsorption and Reorganization on Nanoparticles Probed by the Coffee-Ring Effect: Application to Single Point Mutation Detection.
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.
authors: Ecole normale supérieure, PSL Research University, UPMC Univ Paris 06, CNRS , Department of Chemistry, PASTEUR, 24 rue Lhomond, 75005 Paris, France.|Sorbonne Universités , UPMC Univ Paris 06, ENS, CNRS, PASTEUR, 75005 Paris, France.
authors: Stéphanie
authors: S
authors: Devineau
authors: Ecole normale supérieure, PSL Research University, UPMC Univ Paris 06, CNRS , Department of Chemistry, PASTEUR, 24 rue Lhomond, 75005 Paris, France.|Sorbonne Universités , UPMC Univ Paris 06, ENS, CNRS, PASTEUR, 75005 Paris, France.
authors: Manos
authors: M
authors: Anyfantakis
authors: LIONS, NIMBE, CEA, CNRS, Université Paris-Saclay , CEA Saclay, 91191 Gif sur Yvette, France.
authors: Laurent
authors: L
authors: Marichal
authors: IMRB-INSERM U955 , 5 rue Gustave Eiffel, 94017 Creteil Cedex, France.
authors: Laurent
authors: L
authors: Kiger
authors: Ecole normale supérieure, PSL Research University, UPMC Univ Paris 06, CNRS , Department of Chemistry, PASTEUR, 24 rue Lhomond, 75005 Paris, France.|Sorbonne Universités , UPMC Univ Paris 06, ENS, CNRS, PASTEUR, 75005 Paris, France.
authors: Mathieu
authors: M
authors: Morel
authors: Ecole normale supérieure, PSL Research University, UPMC Univ Paris 06, CNRS , Department of Chemistry, PASTEUR, 24 rue Lhomond, 75005 Paris, France.|Sorbonne Universités , UPMC Univ Paris 06, ENS, CNRS, PASTEUR, 75005 Paris, France.
authors: Sergii
authors: S
authors: Rudiuk
authors: Ecole normale supérieure, PSL Research University, UPMC Univ Paris 06, CNRS , Department of Chemistry, PASTEUR, 24 rue Lhomond, 75005 Paris, France.|Sorbonne Universités , UPMC Univ Paris 06, ENS, CNRS, PASTEUR, 75005 Paris, France.
authors: Damien
authors: D
authors: Baigl
mesh_terms: D000327:Adsorption; D000328:Adult; D000818:Animals; D002417:Cattle; D006454:Hemoglobins / Q000737:chemistry* / Q000235:genetics*; D006801:Humans; D008958:Models, Molecular; D053758:Nanoparticles / Q000737:chemistry*; D017354:Point Mutation; D011137:Polystyrenes / Q000737:chemistry; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000235:genetics*
chemical_list: D006454:Hemoglobins; D011137:Polystyrenes; D012710:Serum Albumin, Bovine