Person:
Cañadas Benito, Olga

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First Name
Olga
Last Name
Cañadas Benito
URI
https://hdl.handle.net/20.500.14352/74363
Affiliation
Universidad Complutense de Madrid
Faculty / Institute
Ciencias Biológicas
Department
Bioquímica y Biología Molecular
Area
Bioquímica y Biología Molecular
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2004 - 200912010 - 20121
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Author: Casals Carro, María Cristina × Author: Cañadas Benito, Olga × Item Type: Publication × Subject: 577.1 ×

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Now showing 1 - 2 of 2
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    Characterization of liposomal tacrolimus in lung surfactant-like phospholipids and evaluation of its immunosuppressive activity.
    (Biochemistry, 2004) Cañadas Benito, Olga; Guerrero, R; García-Cañero, R; Orellana Moraleda, Guillermo; Menéndez, M; Casals Carro, María Cristina
    Tacrolimus (FK506) is a hydrophobic immunosuppressive agent that rapidly penetrates the plasmatic membrane and inhibits the signal transduction cascade of T lymphocytes. The objective of this study was the characterization of liposomal FK506 with surfactant-like phospholipids to be administered intratracheally after lung transplantation or in inflammatory lung diseases. We evaluated the optimal incorporation of FK506 in dipalmitoylphosphatidylcholine (DPPC) and DPPC/1-palmitoyl-2-oleoylphosphatidylglycerol (POPG) monolayers and bilayers and the effects of FK506 on the physical properties of DPPC and DPPC/POPG (8:2 w/w) vesicles. In addition, we assessed the immunosuppressive effects of surfactant-like phospholipid vesicles containing different amounts of FK506 on T-cell proliferation and interleukin 2 production. From surface pressure measurements of FK506/DPPC and FK506/DPPC/POPG mixed monolayers, we determined that FK506 was embedded into these monolayers up to an FK506 concentration of about 0.4 mol %. Beyond this concentration, FK506 was not quantitatively incorporated into the monolayer, suggesting possible concentration-dependent aggregation of tacrolimus. The incorporation of FK506 into DPPC monolayers, at concentrations
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    Differential scanning calorimetry of protein-lipid interactions
    (Lipid-protein interactions: Methods and Protocols, 2012) Cañadas Benito, Olga; Casals Carro, María Cristina; Kleinchmidt, Jorg
    Differential scanning calorimetry (DSC) is a highly sensitive non-perturbing technique for measuring the thermodynamic properties of thermally induced transitions. This technique is particularly useful for the characterization of lipid/protein interactions. This chapter presents an introduction to DSC instrumentation, basic theory, and methods and describes DSC applications for characterizing protein effects on model lipid membranes. Examples of the use of DSC for the evaluation of protein effects on modulation of membrane domains and membrane stability are given.