Signature pattern formation in drying globular protein solution droplets: understanding self-assembled macroscopic states as indicators of the initial microscopic states.

The drying process, self-assembly of the proteins and the phase separation of a thermotropic liquid crystal (LC) from an initial aqueous solution represent a rich area of study. A focus of this work is to compare the behavior of two different proteins, bovine serum albumin [BSA] and lysozyme [Lys] in the ternary system through optical microscopy. During the drying process, the intensity profile shows three regimes in the presence of LC whereas no intensity variation is observed in its absence in both protein drops. The striking outcome is the presence of an umbilical defect of [+1] strength in every domain near the edge of BSA drop, whereas, each domain has a central dark region surrounded by a bright region in the dried Lys drop. Finally, the crack spacing in the dried Lys drop is reduced in the presence of LC whereas, no significant difference is found in the dried BSA drop.

The drying of bio-colloidal droplets can be used in many medical and forensic applications. The whole human blood is the most complex bio-colloid system, whereas bovine serum albumin (BSA) is the simplest. This paper focuses on the drying characteristics and the final morphology of these two bio-colloids. The experiments were conducted by varying their initial concentrations, and the solutions were dried under various controlled substrate temperatures using optical and scanning electron microscopy. The droplet parameters (the contact angle, the fluid front, and the first-order image statistics) reveal the drying process’s unique features. Interestingly, both BSA and blood drying droplets’ contact angle measurements show evidence of a concentration-driven transition as the behavior changes from non-monotonic to monotonic decrease. This result indicates that this transition behavior is not limited to multi-component bio-colloid (blood) only, but may be a phenomenon of a bio-colloidal solution containing a large number of interacting components. The high dilution of blood behaves like the BSA solution. The ring-like deposition, the crack morphology, and the microstructures suggest that the components have enough time to segregate and deposit onto the substrate under ambient conditions. However, there is insufficient time for evaporative-driven segregation to occur at elevated temperatures, as expected.

Multi-colloidal systems exhibit a variety of structural and functional complexity owing to their ability to interact amongst different components into self-assembled structures. This paper presents experimental confirmations that reveal an interesting sharp phase transition during the drying state and in the dried film as a function of diluting concentrations ranging from 100% (undiluted whole blood) to 12.5% (diluted concentrations). An additional complementary contact angle measurement exhibits a monotonic decrease with a peak as a function of drying. This peak is related to a change in visco-elasticity that decreases with dilution, and disappears at the dilution concentration for the observed phase transition equivalent to 62% (v/v). This unique behavior is clearly commensurate with the optical image statistics and morphological analysis; and it is driven by the decrease in the interactions between various components within this bio-colloid. The implications of these phenomenal systems may address many open-ended questions of complex hierarchical structures.

Abstract