The affinity of histamine to serum albumin: Capillary electrophoresis‐frontal analysis and in‐silico molecular docking approaches

Abstract

Histamine is a biogenic amine found in various body tissues and responsible for many critical vital activities. It is also responsible for allergic reactions in the body. Ingestion of foods containing high amounts of histamine can cause fatal allergic reactions. Albumin in plasma controls drugs and free concentrations of bioactive constituents taken to the body with food. Hence, this study aimed to characterise the interactions of histamine with bovine serum albumin. Capillary electrophoresis in the frontal analysis mode was employed in this study as a practical approach for assessing histamine‐bovine serum albumin affinity. The plateau‐shaped free histamine peak was well separated from the bovine serum albumin (BSA)‐histamine complex peak. The free histamine concentration was obtained by following the height of the free histamine peak. Whereas the bound histamine concentrations were obtained by calculating the difference between the height of total and free histamine peaks. Histamine bound to BSA at one independent site with a Kb value of 2.50 × 103 L/mol. Moreover, an in‐silico molecular docking method was performed, and it was revealed that the binding site of histamine was located closer to Lysine‐131 in subdomain IIA of bovine serum albumin.