Study examines surface structure of serum albumin films using atomic force microscopy, suggesting new insights into biofluid properties.
Establishing the relationship between the properties of a biological fluid solution at the molecular level and the structural features and physicochemical properties of the self-organization of films as a result of their dehydration is one of the most important problems of modern biomedical technologies. The glassy part of a dehydrated film of human serum albumin was studied using atomic force microscopy (AFM). The structure of the water-protein matrix was visualized, and an approach to interpreting AFM images was proposed. Primary and secondary structural elements of the protein gel were revealed. An algorithm for assessing quantitatively the albumin film structure, allowing one to determine many parameters of protein formations at the molecular and supramolecular levels, is considered. This approach opens up new possibilities in studying the mechanism of structure formation in biofluids.
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Buzoverya et al. (2026) studied this question.
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