The interaction and binding of flavonoids to human serum albumin modify its conformation, stability and resistance against aggregation and oxidative injuries

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• 作者：Davide Barreca^a ; Giuseppina Laganà ; ^a ; Giovanni Toscano^a ; Pietro Calandra^b ; Mikhail A. Kiselev^c ; Domenico Lombardo^d ; Ersilia Bellocco^a ; ^{ebellocco@unime.it}
• 关键词：Flavonoid ; Human serum albumin ; FTIR ; Fluorescence ; Oxidative stresses and protein fibrillation ; Thermodynamic and kinetic variations.
• 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1861
• 期：1
• 页码：3531-3539
• 全文大小：1115 K
• 卷排序：1861

文摘

Phloretin–HSA complex formation involves property changes in both compounds. Phloretin binds to protein in subdomain IIA. Phloretin modifies the secondary structure of HSA Phloretin–HSA complex is able to withstand degradation due to HCLO and fibrillation.