Determination of driving forces for bovine serum albumin-Ponceau4R binding using surface plasmon resonance and fluorescence spectroscopy: a comparative study

Página do item simplificado
dc.creatorCarini Aparecida Lelis
dc.creatorGabriel Max Dias Ferreira
dc.creatorGuilherme Max Dias Ferreira
dc.creatorMaria do Carmo Hespanhol
dc.creatorMaximiliano Soares Pinto
dc.creatorLuis Henrique Mendes da Silva
dc.creatorAna Clarissa dos Santos Pires
dc.date.accessioned2022-04-04T11:49:40Z
dc.date.accessioned2025-09-09T01:27:27Z
dc.date.available2022-04-04T11:49:40Z
dc.date.issued2017-09
dc.description.sponsorshipOutra Agência
dc.identifier.doihttps://doi.org/10.1016/j.foodhyd.2017.03.027
dc.identifier.issn0268005X
dc.identifier.urihttps://hdl.handle.net/1843/40728
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofFood Hydrocolloids
dc.rightsAcesso Restrito
dc.subjectAlbumina
dc.subjectRessonância
dc.subjectEspectroscopia de fluorescência
dc.subjectEntropia
dc.subjectEntalpia
dc.subjectCorantes sintéticos
dc.titleDetermination of driving forces for bovine serum albumin-Ponceau4R binding using surface plasmon resonance and fluorescence spectroscopy: a comparative study
dc.typeArtigo de periódico
local.citation.epage35
local.citation.spage29
local.citation.volume70
local.description.resumoPonceau 4R (P4R) and bovine serum albumin (BSA) may interact changing food properties. We compared fluorescence spectroscopy and surface plasmon resonance (SPR) for studying, in vitro, the interactions between BSA and P4R at pH 7.4 and 3.5 in different temperatures. Fluorescence data pointed to the formation of a complex where P4R was bound on site I or II of BSA, with a stoichiometry around one and a binding constant (Kb) ranging from 1.37 × 105 to 20.15 × 106 L mol−1. The complex formation at both pH was enthalpically driven (standard enthalpy change, ΔH°F = −60.69 and −63.06 kJ mol−1, for pH 7.4 and 3.5, respectively). Using SPR, we also found the formation of 1:1 BSA-P4R complexes, but the calculated Kb values were much smaller, on the order of 103 L mol−1. Again, we found that the formation of BSA-P4R complex was driven by enthalpy decreasing; however the standard enthalpy change was less negative than that found by fluorescence (ΔH°SPR = −15.05 and −40.55 kJ mol−1, at pH 7.4 and 3.5, respectively). Our results show that these distinct techniques provided different thermodynamic binding parameters for the BSA-P4R interaction, especially regarding ΔH° values, indicating that BSA-P4R binding was a multisite phenomenon, and that sites far from tryptophan residues were the main responsible by electrostatic interaction. Thus, this work clearly shows the importance of using complementary techniques for a complete thermodynamic characterization of complexes formed between azo-colorants and proteins; which is directly related to physicochemical properties of systems containing both molecules together.
local.publisher.countryBrasil
local.publisher.departmentICA - INSTITUTO DE CIÊNCIAS AGRÁRIAS
local.publisher.initialsUFMG
local.url.externahttps://www.sciencedirect.com/science/article/pii/S0268005X16306075?via%3Dihub

Arquivos

Licença do pacote

Agora exibindo 1 - 1 de 1
Imagem de Miniatura
Nome:
License.txt
Tamanho:
1.99 KB
Formato:
Plain Text
Descrição:
Baixar

Coleções

Artigo de Periódico

Logo UFMG