The investigation of antigen-laden droplet deposition patterns on antibody-immobilized substrates has potential for disease detection. Stationary droplets that contain antigens on surfaces immobilized with antibodies can function as microreactors. Temperature modulation enhances reaction efficiency and reduces detection time in droplet-based systems. Thus, the aim of this study is to explore the impact of substrate heating on the structures of protein deposits and the influence of substrate temperature on thermo-solutal Marangoni convection within the droplets. Previous research has explored deposition patterns as diagnostic tools, but limited investigations have focused on the effects of substrate heating on protein deposit structures and the influence of substrate temperature on thermo-solutal Marangoni convection within droplets, creating a knowledge gap. In this study, we conducted experiments to explore how heating the substrate affects the deposition patterns of droplets containing prostate-specific antigen (PSA) on a substrate immobilized with anti-PSA IgG. Additionally, we investigated the thermo-solutal Marangoni convection within these droplets. Our findings reveal distinct deposition patterns classified into dendritic structures (heterogeneous), transitional patterns, and needle-like (homogeneous) structures. The presence of prominent coffee rings and the variation in crystal size across different groups highlight the interplay between thermal and solutal Marangoni advection. Entropy analysis provides insights into structural differences within and between patterns. This work optimizes substrate temperatures for reduced evaporation and detection times while preserving protein integrity, advancing diagnostic tool development, and improving understanding of droplet-based systems.

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