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  1. Article ; Online: Differential Scanning Calorimetry of Protein-Lipid Interactions.

    Cañadas, Olga / Casals, Cristina

    Methods in molecular biology (Clifton, N.J.)

    2019  Volume 2003, Page(s) 91–106

    Abstract: Differential scanning calorimetry (DSC) is a highly sensitive nonperturbing technique used for studying the thermodynamic properties of thermally induced transitions. Since these properties might be affected by ligand binding, DSC is particularly useful ... ...

    Abstract Differential scanning calorimetry (DSC) is a highly sensitive nonperturbing technique used for studying the thermodynamic properties of thermally induced transitions. Since these properties might be affected by ligand binding, DSC is particularly useful for the characterization of protein interactions with biomimetic membranes. The advantages of this technique over other methods consist in the direct measurement of intrinsic thermal properties of the samples, requiring no chemical modifications or extrinsic probes. This chapter describes the basic theory of DSC and provides the reader with an understanding of the capabilities of DSC instrumentation and the type of information that can be achieved from DSC studies of lipid-protein interactions. In particular, the chapter provides a detailed analysis of DSC data to assess the effects of proteins on biomimetic membranes.
    MeSH term(s) Biomimetics/methods ; Calorimetry, Differential Scanning/methods ; Ligands ; Lipids/chemistry ; Membranes/metabolism ; Proteins/metabolism ; Thermodynamics
    Chemical Substances Ligands ; Lipids ; Proteins
    Language English
    Publishing date 2019-05-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-9512-7_5
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  2. Article: Pulmonary surfactant inactivation by β-D-glucan and protective role of surfactant protein A

    Cañadas, Olga / Sáenz, Alejandra / de Lorenzo, Alba / Casals, Cristina

    Colloids and surfaces. 2022 Feb., v. 210

    2022  

    Abstract: Pulmonary fungal infections lead to damage of the endogenous lung surfactant system. However, the molecular mechanism underlying surfactant inhibition is unknown. β-D-glucan is the major component of pathogenic fungal cell walls and is also present in ... ...

    Abstract Pulmonary fungal infections lead to damage of the endogenous lung surfactant system. However, the molecular mechanism underlying surfactant inhibition is unknown. β-D-glucan is the major component of pathogenic fungal cell walls and is also present in organic dust, which increases the risk of respiratory diseases. The objective of this study was to characterize the interaction of this D-glucopyranose polymer with pulmonary surfactant. Our results show that β-D-glucan induced a concentration-dependent inhibition of the surface adsorption, respreading, and surface tension-lowering activity of surfactant preparations containing surfactant proteins SP-B and SP-C. Our data support a new mechanism of surfactant inhibition that consists in the extraction of phospholipid molecules from surfactant membranes by β-D-glucan. As a result, surfactant membranes became more fluid, as demonstrated by fluorescence anisotropy, and showed decreased Tₘ and transition enthalpy. Surfactant preparations containing surfactant protein A (SP-A) were more resistant to β-D-glucan inhibition. SP-A bound to different β-D-glucans with high affinity (Kd = 1.5 ± 0.1 nM), preventing and reverting β-D-glucan inhibitory effects on surfactant interfacial adsorption and partially abrogating β-D-glucan inhibitory effects on surfactant’s reduction of surface tension. We conclude that β-D-glucan inhibits the biophysical function of surfactant preparations lacking SP-A by subtraction of phospholipids from surfactant bilayers and monolayers. The increased resistance of SP-A-containing surfactant preparations to β-D-glucan reinforces its use in surfactant replacement therapy.
    Keywords adsorption ; anisotropy ; dust ; enthalpy ; fluorescence ; fungi ; lungs ; phospholipids ; polymers ; protective effect ; risk ; surface tension ; surfactant proteins ; surfactants ; therapeutics
    Language English
    Dates of publication 2022-02
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 1500523-9
    ISSN 1873-4367 ; 0927-7765
    ISSN (online) 1873-4367
    ISSN 0927-7765
    DOI 10.1016/j.colsurfb.2021.112237
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Pulmonary surfactant inactivation by β-D-glucan and protective role of surfactant protein A.

    Cañadas, Olga / Sáenz, Alejandra / de Lorenzo, Alba / Casals, Cristina

    Colloids and surfaces. B, Biointerfaces

    2021  Volume 210, Page(s) 112237

    Abstract: Pulmonary fungal infections lead to damage of the endogenous lung surfactant system. However, the molecular mechanism underlying surfactant inhibition is unknown. β-D-glucan is the major component of pathogenic fungal cell walls and is also present in ... ...

    Abstract Pulmonary fungal infections lead to damage of the endogenous lung surfactant system. However, the molecular mechanism underlying surfactant inhibition is unknown. β-D-glucan is the major component of pathogenic fungal cell walls and is also present in organic dust, which increases the risk of respiratory diseases. The objective of this study was to characterize the interaction of this D-glucopyranose polymer with pulmonary surfactant. Our results show that β-D-glucan induced a concentration-dependent inhibition of the surface adsorption, respreading, and surface tension-lowering activity of surfactant preparations containing surfactant proteins SP-B and SP-C. Our data support a new mechanism of surfactant inhibition that consists in the extraction of phospholipid molecules from surfactant membranes by β-D-glucan. As a result, surfactant membranes became more fluid, as demonstrated by fluorescence anisotropy, and showed decreased T
    MeSH term(s) Glucans ; Phospholipids ; Pulmonary Surfactant-Associated Protein A ; Pulmonary Surfactant-Associated Protein B ; Pulmonary Surfactants
    Chemical Substances Glucans ; Phospholipids ; Pulmonary Surfactant-Associated Protein A ; Pulmonary Surfactant-Associated Protein B ; Pulmonary Surfactants
    Language English
    Publishing date 2021-11-21
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1500523-9
    ISSN 1873-4367 ; 0927-7765
    ISSN (online) 1873-4367
    ISSN 0927-7765
    DOI 10.1016/j.colsurfb.2021.112237
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Synergistic Action of Antimicrobial Lung Proteins against

    Fraile-Ágreda, Víctor / Cañadas, Olga / Weaver, Timothy E / Casals, Cristina

    International journal of molecular sciences

    2021  Volume 22, Issue 20

    Abstract: As key components of innate immunity, lung antimicrobial proteins play a critical role in warding off invading respiratory pathogens. Lung surfactant protein A (SP-A) exerts synergistic antimicrobial activity with ... ...

    Abstract As key components of innate immunity, lung antimicrobial proteins play a critical role in warding off invading respiratory pathogens. Lung surfactant protein A (SP-A) exerts synergistic antimicrobial activity with the
    MeSH term(s) Anti-Bacterial Agents/metabolism ; Anti-Bacterial Agents/pharmacology ; Bronchoalveolar Lavage Fluid/chemistry ; Drug Synergism ; Humans ; Immunity, Innate/physiology ; Klebsiella Infections/pathology ; Klebsiella Infections/prevention & control ; Klebsiella pneumoniae/drug effects ; Klebsiella pneumoniae/immunology ; Lung/chemistry ; Lung/immunology ; Lung/metabolism ; Lung/microbiology ; Microbial Sensitivity Tests ; Pulmonary Surfactant-Associated Protein A/isolation & purification ; Pulmonary Surfactant-Associated Protein A/metabolism ; Pulmonary Surfactant-Associated Protein A/pharmacology ; Pulmonary Surfactants/isolation & purification ; Pulmonary Surfactants/metabolism ; Pulmonary Surfactants/pharmacology ; Respiratory Tract Infections/pathology ; Respiratory Tract Infections/prevention & control
    Chemical Substances Anti-Bacterial Agents ; Pulmonary Surfactant-Associated Protein A ; Pulmonary Surfactants
    Language English
    Publishing date 2021-10-15
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms222011146
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Lipid-Protein and Protein-Protein Interactions in the Pulmonary Surfactant System and Their Role in Lung Homeostasis.

    Cañadas, Olga / Olmeda, Bárbara / Alonso, Alejandro / Pérez-Gil, Jesús

    International journal of molecular sciences

    2020  Volume 21, Issue 10

    Abstract: Pulmonary surfactant is a lipid/protein complex synthesized by the alveolar epithelium and secreted into the airspaces, where it coats and protects the large respiratory air-liquid interface. Surfactant, assembled as a complex network of membranous ... ...

    Abstract Pulmonary surfactant is a lipid/protein complex synthesized by the alveolar epithelium and secreted into the airspaces, where it coats and protects the large respiratory air-liquid interface. Surfactant, assembled as a complex network of membranous structures, integrates elements in charge of reducing surface tension to a minimum along the breathing cycle, thus maintaining a large surface open to gas exchange and also protecting the lung and the body from the entrance of a myriad of potentially pathogenic entities. Different molecules in the surfactant establish a multivalent crosstalk with the epithelium, the immune system and the lung microbiota, constituting a crucial platform to sustain homeostasis, under health and disease. This review summarizes some of the most important molecules and interactions within lung surfactant and how multiple lipid-protein and protein-protein interactions contribute to the proper maintenance of an operative respiratory surface.
    MeSH term(s) Alveolar Epithelial Cells/metabolism ; Alveolar Epithelial Cells/microbiology ; Alveolar Epithelial Cells/physiology ; Animals ; Homeostasis ; Humans ; Lipid Metabolism ; Pulmonary Surfactant-Associated Proteins/metabolism
    Chemical Substances Pulmonary Surfactant-Associated Proteins
    Keywords covid19
    Language English
    Publishing date 2020-05-25
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms21103708
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  6. Article: Polyhydroxyalkanoate Nanoparticles for Pulmonary Drug Delivery: Interaction with Lung Surfactant.

    Cañadas, Olga / García-García, Andrea / Prieto, M Auxiliadora / Pérez-Gil, Jesús

    Nanomaterials (Basel, Switzerland)

    2021  Volume 11, Issue 6

    Abstract: Polyhydroxyalkanoates (PHA) are polyesters produced intracellularly by many bacterial species as energy storage materials, which are used in biomedical applications, including drug delivery systems, due to their biocompatibility and biodegradability. In ... ...

    Abstract Polyhydroxyalkanoates (PHA) are polyesters produced intracellularly by many bacterial species as energy storage materials, which are used in biomedical applications, including drug delivery systems, due to their biocompatibility and biodegradability. In this study, we evaluated the potential application of this nanomaterial as a basis of inhaled drug delivery systems. To that end, we assessed the possible interaction between PHA nanoparticles (NPs) and pulmonary surfactant using dynamic light scattering, Langmuir balances, and epifluorescence microscopy. Our results demonstrate that NPs deposited onto preformed monolayers of DPPC or DPPC/POPG bind these surfactant lipids. This interaction facilitated the translocation of the nanomaterial towards the aqueous subphase, with the subsequent loss of lipid from the interface. NPs that remained at the interface associated with liquid expanded (LE)/tilted condensed (TC) phase boundaries, decreasing the size of condensed domains and promoting the intermixing of TC and LE phases at submicroscopic scale. This provided the stability necessary for attaining high surface pressures upon compression, countering the destabilization induced by lipid loss. These effects were observed only for high NP loads, suggesting a limit for the use of these NPs in pulmonary drug delivery.
    Language English
    Publishing date 2021-06-03
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2662255-5
    ISSN 2079-4991
    ISSN 2079-4991
    DOI 10.3390/nano11061482
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  7. Article ; Online: Lipid–Protein and Protein–Protein Interactions in the Pulmonary Surfactant System and Their Role in Lung Homeostasis

    Olga Cañadas / Bárbara Olmeda / Alejandro Alonso / Jesús Pérez-Gil

    International Journal of Molecular Sciences, Vol 21, Iss 3708, p

    2020  Volume 3708

    Abstract: Pulmonary surfactant is a lipid/protein complex synthesized by the alveolar epithelium and secreted into the airspaces, where it coats and protects the large respiratory air–liquid interface. Surfactant, assembled as a complex network of membranous ... ...

    Abstract Pulmonary surfactant is a lipid/protein complex synthesized by the alveolar epithelium and secreted into the airspaces, where it coats and protects the large respiratory air–liquid interface. Surfactant, assembled as a complex network of membranous structures, integrates elements in charge of reducing surface tension to a minimum along the breathing cycle, thus maintaining a large surface open to gas exchange and also protecting the lung and the body from the entrance of a myriad of potentially pathogenic entities. Different molecules in the surfactant establish a multivalent crosstalk with the epithelium, the immune system and the lung microbiota, constituting a crucial platform to sustain homeostasis, under health and disease. This review summarizes some of the most important molecules and interactions within lung surfactant and how multiple lipid–protein and protein–protein interactions contribute to the proper maintenance of an operative respiratory surface.
    Keywords pulmonary surfactant film ; surfactant metabolism ; surface tension ; respiratory air–liquid interface ; inflammation ; antimicrobial activity ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 612
    Language English
    Publishing date 2020-05-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Polyhydroxyalkanoate Nanoparticles for Pulmonary Drug Delivery

    Olga Cañadas / Andrea García-García / M. Auxiliadora Prieto / Jesús Pérez-Gil

    Nanomaterials, Vol 11, Iss 1482, p

    Interaction with Lung Surfactant

    2021  Volume 1482

    Abstract: Polyhydroxyalkanoates (PHA) are polyesters produced intracellularly by many bacterial species as energy storage materials, which are used in biomedical applications, including drug delivery systems, due to their biocompatibility and biodegradability. In ... ...

    Abstract Polyhydroxyalkanoates (PHA) are polyesters produced intracellularly by many bacterial species as energy storage materials, which are used in biomedical applications, including drug delivery systems, due to their biocompatibility and biodegradability. In this study, we evaluated the potential application of this nanomaterial as a basis of inhaled drug delivery systems. To that end, we assessed the possible interaction between PHA nanoparticles (NPs) and pulmonary surfactant using dynamic light scattering, Langmuir balances, and epifluorescence microscopy. Our results demonstrate that NPs deposited onto preformed monolayers of DPPC or DPPC/POPG bind these surfactant lipids. This interaction facilitated the translocation of the nanomaterial towards the aqueous subphase, with the subsequent loss of lipid from the interface. NPs that remained at the interface associated with liquid expanded (LE)/tilted condensed (TC) phase boundaries, decreasing the size of condensed domains and promoting the intermixing of TC and LE phases at submicroscopic scale. This provided the stability necessary for attaining high surface pressures upon compression, countering the destabilization induced by lipid loss. These effects were observed only for high NP loads, suggesting a limit for the use of these NPs in pulmonary drug delivery.
    Keywords DPPC ; POPG ; PHA ; dynamic light scattering ; lipid monolayers ; relaxation kinetics ; Chemistry ; QD1-999
    Subject code 620
    Language English
    Publishing date 2021-06-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Differential scanning calorimetry of protein-lipid interactions.

    Cañadas, Olga / Casals, Cristina

    Methods in molecular biology (Clifton, N.J.)

    2013  Volume 974, Page(s) 55–71

    Abstract: 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 ... ...

    Abstract 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.
    MeSH term(s) Calorimetry, Differential Scanning/methods ; Humans ; Lipid Bilayers/metabolism ; Lipid Metabolism ; Protein Binding ; Proteolipids/metabolism ; Pulmonary Surfactant-Associated Protein A/metabolism
    Chemical Substances Lipid Bilayers ; Proteolipids ; Pulmonary Surfactant-Associated Protein A ; proteoliposomes
    Language English
    Publishing date 2013
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-62703-275-9_4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Lipid-Protein and Protein-Protein Interactions in the Pulmonary Surfactant System and Their Role in Lung Homeostasis

    Cañadas, Olga / Olmeda, Bárbara / Alonso, Alejandro / Pérez-Gil, Jesús

    Abstract: Pulmonary surfactant is a lipid/protein complex synthesized by the alveolar epithelium and secreted into the airspaces, where it coats and protects the large respiratory air-liquid interface. Surfactant, assembled as a complex network of membranous ... ...

    Abstract Pulmonary surfactant is a lipid/protein complex synthesized by the alveolar epithelium and secreted into the airspaces, where it coats and protects the large respiratory air-liquid interface. Surfactant, assembled as a complex network of membranous structures, integrates elements in charge of reducing surface tension to a minimum along the breathing cycle, thus maintaining a large surface open to gas exchange and also protecting the lung and the body from the entrance of a myriad of potentially pathogenic entities. Different molecules in the surfactant establish a multivalent crosstalk with the epithelium, the immune system and the lung microbiota, constituting a crucial platform to sustain homeostasis, under health and disease. This review summarizes some of the most important molecules and interactions within lung surfactant and how multiple lipid-protein and protein-protein interactions contribute to the proper maintenance of an operative respiratory surface.
    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #361420
    Database COVID19

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