Protein adsorption on solid materials plays a central role in analytical, biomedical, and separation‐based technologies. Depending on the application, protein–surface interactions may be exploited for selective capture or must be minimized to avoid nonspecific fouling. This review examines the fundamental mechanisms governing protein adsorption on solid surfaces, with emphasis on hydrophobic and electrostatic interactions, hydrogen bonding, π–π stacking, and confinement effects in porous materials. We discuss how material properties such as surface chemistry, porosity, and mineral composition influence protein binding, with particular focus on carbon‐based and inorganic solids. Strategies for controlling protein–surface interactions through surface functionalization, polymer modification, and affinity‐based approaches are critically reviewed. Special attention is given to molecularly imprinted polymers and aptamer‐functionalized materials as routes to introduce molecular selectivity beyond nonspecific adsorption. Finally, representative applications in biosensing, selective adsorption, and solid‐phase extraction are summarized, highlighting current capabilities and limitations of protein‐interactive materials in analytical workflows.
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Kowalczyk et al. (2026) studied this question.
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