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|metadata.artigo.dc.title:||Lactoferrin denaturation induced by anionic surfactants: the role of the ferric ion in the protein stabilization|
|metadata.artigo.dc.creator:||Ferreira, Gabriel Max Dias|
Ferreira, Guilherme Max Dias
Agudelo, Álvaro Javier Patiño
Hudson, Eliara Acipreste
Pires, Ana Clarissa dos Santos
Silva, Luis Henrique Mendes da
|metadata.artigo.dc.identifier.citation:||FERREIRA, G. M. D. et al. Lactoferrin denaturation induced by anionic surfactants: the role of the ferric ion in the protein stabilization. International Journal of Biological Macromolecules, [S.l.], v. 117, p. 1039-1049, Oct. 2018.|
|metadata.artigo.dc.description.abstract:||Here, investigation was made of the interaction between lactoferrin (Lf) and the anionic surfactants sodium dodecyl sulfate (SDS), sodium dodecylbenzene sulfonate (SDBS), and sodium decyl sulfate (DSS), using isothermal titration calorimetry, Nano differential scanning calorimetry (NanoDSC), and fluorescence spectroscopy. The Lf-surfactant interaction was enthalpically favorable (the integral enthalpy change ranged from −5.99 kJ mol−1, for SDS at pH 3.0, to −0.61 kJ mol−1, for DSS at pH 12.0) and promoted denaturation of the protein. The Lf denaturation efficiency followed the order DSS < SDS < SDBS. The adsorption capacity of the protein with respect to surfactant strongly depended on pH and the surfactant structure, reaching a maximum value of 505 SDBS molecules per gram of Lf at pH 3.0. The different efficiencies of the surfactants in denaturing Lf were attributed to the balance of hydrophobic and electrostatic interactions, which also depended on pH and the surfactant structure, highlighting the SDBS-tryptophan residue specific interaction, where SDBS acted as a quencher of fluorescence. Interestingly, the NanoDSC and fluorescence measurements showed that the ferric ion bound to Lf increased its stability against denaturation induced by the surfactants. The results have important implications for understanding the influence of surfactants on structural changes in metalloproteins.|
|Appears in Collections:||DQI - Artigos publicados em periódicos|
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