Interaction of cinnamic acid and methyl cinnamate with bovine serum albumin: A thermodynamic approach.

Natália Moreira Nunes, Ana Flávia Coelho Pacheco, Álvaro Javier Patiño Agudelo, Luis Henrique Mendes da Silva, Maximiliano Soares Pinto, Maria do Carmo Hespanhol, Ana Clarissa Dos Santos Pires

Food chemistry 2017 Dec 15

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Cinnamic acid (CA) and methyl cinnamate (MC) have attracted interest of researchers because of their broad therapeutic functions. Here, we investigated the interaction of CA and MC with bovine serum albumin (BSA) at pH 3.5, 5.0, and 7.4 using fluorescence spectroscopy, differential scanning nanocalorimetry, and measurements of interfacial tension, size, and zeta potential. BSA formed a complex with the ligands with stoichiometry of approximately 1.0. At pH 7.4, CA-BSA complex formation was entropically driven. The interaction between MC and BSA was more favorable than with CA and was enthalpically driven under the same conditions. The pH played an important role in BSA conformation, which altered the manner in which it interacts with the ligands. Interestingly, both CA and MC had no effect on the surface tension of BSA/air interfaces. These data contribute to the knowledge of CA/MC-BSA interactions and provide important data for application in the food industry. Copyright © 2017 Elsevier Ltd. All rights reserved.

Citation

Natália Moreira Nunes, Ana Flávia Coelho Pacheco, Álvaro Javier Patiño Agudelo, Luis Henrique Mendes da Silva, Maximiliano Soares Pinto, Maria do Carmo Hespanhol, Ana Clarissa Dos Santos Pires. Interaction of cinnamic acid and methyl cinnamate with bovine serum albumin: A thermodynamic approach. Food chemistry. 2017 Dec 15;237:525-531