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

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dc.creatorNatália Moreira Nunes
dc.creatorAna Flávia Coelho Pacheco
dc.creatorÁlvaro Javier Patiño Agudelo
dc.creatorLuis Henrique Mendes da Silva
dc.creatorMaximiliano Soares Pinto
dc.creatorMaria do Carmo Hespanhol
dc.creatorAna Clarissa dos Santos Pires
dc.date.accessioned2022-03-31T12:00:58Z
dc.date.accessioned2025-09-09T01:13:03Z
dc.date.available2022-03-31T12:00:58Z
dc.date.issued2017-12-15
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológico
dc.description.sponsorshipFAPEMIG - Fundação de Amparo à Pesquisa do Estado de Minas Gerais
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
dc.identifier.doihttps://doi.org/10.1016/j.foodchem.2017.05.131
dc.identifier.issn03088146
dc.identifier.urihttps://hdl.handle.net/1843/40650
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofFood Chemistry
dc.rightsAcesso Restrito
dc.subjectAlbumina
dc.subjectEspectroscopia de fluorescência
dc.subjectCalorimetria
dc.subjectEstequiometria
dc.titleInteraction of cinnamic acid and methyl cinnamate with bovine serum albumin: a thermodynamic approach
dc.typeArtigo de periódico
local.citation.epage531
local.citation.spage525
local.citation.volume237
local.description.resumoCinnamic 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.
local.publisher.countryBrasil
local.publisher.departmentICA - INSTITUTO DE CIÊNCIAS AGRÁRIAS
local.publisher.initialsUFMG
local.url.externahttps://www.sciencedirect.com/science/article/pii/S0308814617309445

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