Salt-induced pattern formation in evaporating droplets of lysozyme solutions.

Solute self-organization during evaporation of colloidal sessile droplets has attracted the attention of researchers over the past few decades due to a variety of technological applications. Recently, pattern formation during evaporation of various biofluids has been studied due to potential applications in screening and diagnosis. The complex morphological patterns in the deposit are unique to various disorders and are influenced by various physical mechanisms occurring during evaporation. These complex patterns can be better understood by studying evaporation of model solutions of biological relevance. Here, we examine the general features of pattern formation during sessile droplet evaporation of aqueous lysozyme solutions with varying concentrations of NaCl. Lysozyme is a globular protein found in biological fluids such as tears and saliva. The morphological evolution of the droplet is studied by time-lapse video during evaporation via reflection optical microscopy. The final deposits exhibit an amorphous peripheral ring and interior regions containing crystallites and dendritic forms, dependent on NaCl concentration. Scanning electron microscopy (SEM) images demonstrate the multi-scale hierarchical nature of these structures.

Characteristic size for onset of coffee-ring effect in evaporating lysozyme-water solution droplets.

Liquid droplets containing suspended particles deposited on a solid surface often form a ring-like structure due to the redistribution of solute during evaporation, a phenomenon known as the "coffee ring effect". The complex patterns left on the substrate after evaporation are characteristic of the nature of the solute and the particle transport mechanisms. In this study, the morphological evolution and conditions for coffee ring formation for simplified model biological solutions of DI water and lysozyme are examined by AFM and optical microscopy. Lysozyme is a globular protein found in high concentration, for example, in human tears and saliva. The drop diameters studied are very small, ranging from 1 to 50 µm. In this size range, protein motion and the resulting dried residue morphology are highly influenced by the decreased evaporation time of the drop. In this work, we consider the effect of droplet size and concentration on the morphology of the deposited drop as well as the minimal conditions for coffee ring formation in this system. Two distinct deposit types are observed: a simple cap-shaped deposit for drops with small diameters and a ring-like deposit at larger diameters. Ring formation occurs at a critical diameter, which depends systematically on initial lysozyme concentration.

Lysozyme pattern formation in evaporating drops.

Liquid droplets containing suspended particles deposited on a solid, flat surface generally form ringlike structures due to the redistribution of solute during evaporation (the "coffee ring effect"). The forms of the deposited patterns depend on interactions between solute(s), solvent, and substrate. In this study, deposition patterns from droplets of a simplified model biological fluid (DI water + lysozyme) are examined by scanning probe and optical microscopy. The overall lysozyme residue morphology is complex (with both a perimeter "rim" and undulating interior) but varies little with concentration. However, the final packing of lysozyme molecules is strongly dependent on initial concentration.