A Comparative Study of the Drying Evolution and Dried Morphology of two Globular Protein and De-ionized water Solutions

TL;DR

This study investigates how drying dynamics and crack patterns of globular protein solutions, specifically lysozyme and BSA, depend on concentration, revealing distinct morphological features and a fingerprint-like final pattern linked to initial conditions.

Contribution

It provides a detailed comparison of drying evolution and crack morphology of lysozyme and BSA solutions, introducing a mechanical model to interpret the dependence on initial solution state.

Findings

Drying mode transitions from constant contact radius to mixed mode.

Formation of a concentration-dependent 'dimple' in the dried structure.

Crack patterns serve as a fingerprint of initial solution conditions.

Abstract

Pattern formation in drying protein droplets continues to attract considerable research attention because it can be linked to specific protein-protein interactions. An extensive study of the drying evolution and the final crack patterns are presented, highlighting the concentration dependence (from 1 to 13 wt%) on two globular proteins, lysozyme (Lys) and bovine serum albumin (BSA), in de-ionized water. The drying evolution starts with a constant contact radius mode and shifts to a mixed mode where both fluid front and contact angle changes. The contact angle monotonically decreases, whereas, the fluid front exhibits two regimes: an initial linear regime and a later nonlinear regime. Unlike the linear regime, the non-linear regime is faster for Lys droplets. This results in the formation of a "mound"-like structure in the central region. A new feature, a "dimple" is observed in this mound which is found to be dependent on the initial concentration. The different crack morphology of BSA and Lys depends strongly on the initial state of the solution and can be interpreted using a simple mechanical model. In fact, when dried under uniform conditions (surface, humidity, temperature, droplet diameter, etc.), the evolution and the final pattern displays as a fingerprint of the initial state.