TY - JOUR
T1 - Insights into the interaction of Bovine Serum Albumin with Surface-Active Ionic Liquids in aqueous solution
AU - Alves, Márcia M. S.
AU - Araújo, João M. M.
AU - Martins, Ivo C.
AU - Pereiro, Ana B.
AU - Archer, Margarida
N1 - info:eu-repo/grantAgreement/EC/H2020/653706/EU#
Financial support from Fundacao para a Ciencia e Tecnologia (FCT) -Ministerio da Ciencia, Tecnologia e Ensiono Superior (MCTES) (Portugal), through grant PD/BD/128201/2016 (M.M.S.A.), Investigador FCT Program 2013 and FCT Program"Concurso de Estimulo Cientifico CEEC" (IF/00772/2013 and CEECIND/01670/2017 respectively, both to I.C.M.), Investigador FCT Program 2014 (IF/00190/2014 to A.B.P., IF/00210/2014 to J.M.M.A. and IF/00656/2014 to M.A.), and projects PTDC/QEQ-EPR/5841/2014, PTDC/QEQ-FTT/3289/2014 and IF/00210/2014/CP1244/CT0003. This work was also supported by the Associate Laboratory for Green Chemistry LAQV which is financed by national funds from FCT/MCTES (UIDB/50006/2020); iNOVA4Health (LISBOA-01-0145-FEDER-007344, co-funded by FEDER under PT2020) and MostMicro Research Unit (financially supported by LISBOA-01-0145-FEDER-007660 funded by FEDER funds through COMPETE2020 (POCI) and by national funds through FCT).
PY - 2021/1/15
Y1 - 2021/1/15
N2 - The unique physicochemical properties of Ionic liquids (ILs) make them very desirable for biomedical applications, namely as surface active ionic liquids (SAILs). SAILs surface activity, intrinsically higher than conventional surfactants, allows them to enhance drug permeability across biomembranes and, thus, become better drug carriers than current solutions. To harvest the full potential of these materials, in-depth studies of ILs interactions with model proteins are necessary to understand the mechanisms controlling these biological processes. Albumin, a key protein of blood serum, is of particular relevance, namely in drug carrier applications. Thus, here we characterize the interaction of bovine serum albumin (BSA) with fluorinated ionic liquids which are SAILs that possess fluorous tags equal to or longer than four carbon atoms. Their impact on BSA stability and structure was evaluated using different biophysical techniques. Differential scanning fluorimetry (DSF) and calorimetry (DSC), as well as circular dichroism (CD), yielded insights on the stabilization and secondary structure of BSA upon incubation with the ILs. Binding dynamics of the interaction were studied by conductimetry and isothermal titration calorimetry (ITC), which give the values of critical aggregation concentration (CAC) of the BSA-IL complex formation, as well as thermodynamic parameters. The results presented herein support the hypothesis that BSA is stabilized and encapsulated in the presence of FILs. Thus, the FILs studied in this work have potential for uses in biomedical applications.
AB - The unique physicochemical properties of Ionic liquids (ILs) make them very desirable for biomedical applications, namely as surface active ionic liquids (SAILs). SAILs surface activity, intrinsically higher than conventional surfactants, allows them to enhance drug permeability across biomembranes and, thus, become better drug carriers than current solutions. To harvest the full potential of these materials, in-depth studies of ILs interactions with model proteins are necessary to understand the mechanisms controlling these biological processes. Albumin, a key protein of blood serum, is of particular relevance, namely in drug carrier applications. Thus, here we characterize the interaction of bovine serum albumin (BSA) with fluorinated ionic liquids which are SAILs that possess fluorous tags equal to or longer than four carbon atoms. Their impact on BSA stability and structure was evaluated using different biophysical techniques. Differential scanning fluorimetry (DSF) and calorimetry (DSC), as well as circular dichroism (CD), yielded insights on the stabilization and secondary structure of BSA upon incubation with the ILs. Binding dynamics of the interaction were studied by conductimetry and isothermal titration calorimetry (ITC), which give the values of critical aggregation concentration (CAC) of the BSA-IL complex formation, as well as thermodynamic parameters. The results presented herein support the hypothesis that BSA is stabilized and encapsulated in the presence of FILs. Thus, the FILs studied in this work have potential for uses in biomedical applications.
KW - Bovine serum albumin
KW - Encapsulation
KW - Fluorinated ionic liquids
KW - Protein interaction
KW - Surface active ionic liquids
UR - http://www.scopus.com/inward/record.url?scp=85093699807&partnerID=8YFLogxK
U2 - 10.1016/j.molliq.2020.114537
DO - 10.1016/j.molliq.2020.114537
M3 - Article
AN - SCOPUS:85093699807
SN - 0167-7322
VL - 322
JO - Journal of Molecular Liquids
JF - Journal of Molecular Liquids
M1 - 114537
ER -