Abstract
Interactions between proteins and drugs can lead to the formation of stable complexes and have important implications for several processes related to human health. These interactions can affect, for example, the distribution, free concentration, biological activity and metabolism of drugs in the bloodstream. This work presents an investigation based on spectrophotometry (UV–Vis) on the interaction of albumin with heparin (HEP) in aqueous solution and in the form of films, under physiological conditions. Results from analytical models, molecular dynamics and calculations of binding constants indicate that increasing temperature leads to a decrease in the molecular interaction of HEP with albumin, with dynamic interaction, and secondary bonds. Morphological analyzes with fractality assessment corroborate the results. Simulation results suggest that the interaction of HEP with the SARS-CoV-2 spike protein should be stronger, with little variation over time. The weak interaction between HEP and albumin contributes to greater availability of the drug, which inhibits viral invasion in addition to disrupting microthrombi that prevent oxygenation in patients infected with SARS-CoV-2. The investigation of biological systems in solutions or in the form of films has allowed the analysis of complex formation using unconventional pharmacokinetic techniques.
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