Effect of methotrexate and its photodegradation products on the temperature induced denaturation of human serum albumin

Effect of the photodegradation of chemotherapeutic agent methotrexate on the denaturation of human serum albumin has been studied by differential scanning calorimetry and fluorimetric measurements. Photoluminescence studies highlighted entropy driven binding of both methotrexate molecules and its degradation products to the albumin molecules. The calorimetric measurements evaluated by the Kissinger method show elevated activation energy in the presence of methotrexate. Similar but moderated enhancement of the activation energy was obtained in the presence of the photodegradation products of methotrexate. These results highlight stabilization of the human serum albumin by the methotrexate drug which finding may contribute to fine tuning of methotrexate applications in therapy. (C) 2020 The Authors. Published by Elsevier B.V.

Automated summary

The study found that both methotrexate and its photodegradation products bind to human serum albumin through entropy-driven interactions, leading to increased stability of the albumin. Additionally, the presence of methotrexate increases the activation energy, which may contribute to fine tuning methotrexate applications in therapy.