Using a computational model based on spectrofluorimetry data, the characteristics of haloperidol’s interaction with HSA and BSA at 25°C and 37°C were investigated. The relative locations of this drug’s major binding sites in albumins were calculated. Haloperidol is a neuroleptic medicine that belongs to the butyrophenone category. It is a conventional or first-generation antipsychotic treatment. The predominant binding site for haloperidol in HSA and BSA appears to be inside the subdomain IB, according to the findings. When the [HPD]/[albumin] ratio was 1/1000, HPD quenched 12.2(0.6) percent of HSA fluorescence and 22.7(0.9) percent of BSA fluorescence at 37°C. HPD was able to quench 58-65 percent of the fluorescence of the two albumins at 37°C when the [HPD]/[albumin] ratio was equal to 2/300. The HPD association constant for HSA fluorescence was found to be in the range of 107 M-1, roughly two orders of magnitude higher than that of risperidone and three orders of magnitude higher than that of clorpromazine and sulpiride.
Author (S) Details
Celia Martins Cortez
Postgraduation Program in Computation Sciences, Rio de Janeiro State University – UERJ, RJ, Brazil and Postgraduation Program in Medical Sciences, Rio de Janeiro State University – UERJ, RJ, Brazil.
Carla Patrícia de Morais E. Coura
Postgraduation Program in Medical Sciences, Rio de Janeiro State University – UERJ, RJ, Brazil.
Erica Tex Paulino
Laboratory of Innovations in Therapies, Teaching and Bioproducts, Oswaldo Cruz Institute, RJ, Brazil.
Viviane Muniz da Silva Fragoso
Laboratory of Innovations in Therapies, Teaching and Bioproducts, Oswaldo Cruz Institute, RJ, Brazil.
Dilson Silva
Postgraduation Program in Medical Sciences, Rio de Janeiro State University – UERJ, RJ, Brazil.
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