Abstract
Biological systems, by nature, are highly complex. These systems exhibit diverse hierarchical spatial and temporal features when driven far from equilibrium. The generated features are susceptible to the initial conditions that largely depend on vast parameter space. Extracting information on their properties and behavior thus becomes far too complex. This work seeks to examine the drying kinetics of the drops containing a globular protein (lysozyme (Lys)), phosphate buffer saline (PBS), and thermotropic liquid crystal (LCs). The drying evolution and the morphological crack patterns of these drops are examined using high-resolution microscopy, textural image analysis, and statistical methods. This study observes that the textural parameters can identify the (i) phase separation of the salts present in the PBS and (ii) the LCs’ birefringence during the drying evolution. This birefringence activities of the LCs slow down when the initial PBS concentration is increased from 0.25 to 1× despite using a fixed volume of LCs. To comprehend such a surprising effect, the combinations of (i) Lys+PBS and (ii) PBS+LCs are thoroughly examined. A phase diagram is established as a function of initial concentrations of Lys and PBS. The scanning electron microscopic images of Lys+PBS reveal that the tuning between lysozyme and salt concentrations in PBS plays a significant role in determining the morphological patterns. The Lys drops with and without LCs exhibit two distinct regions: the peripheral ring (“coffee-ring”) and the central ones. This phase-separated ring formation indicates that the film containing Lys and salts might have formed on top of these LCs in the central region, which reduces the optical response (birefringence) of LCs. A physical mechanism is proposed in this paper to anticipate the redistributions of LCs in a multi-component system such as Lys+PBS+LCs.