Production and characterisation of recombinant forms of human pulmonary surfactant protein C (SP-C): Structure and surface activity
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Production and characterisation of recombinant forms of human pulmonary surfactant protein C (SP-C): Structure and surface activity

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Production and characterisation of recombinant forms of human pulmonary surfactant protein C (SP-C): Structure and surface activity

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dc.contributor.author Lukovic, Dunja
dc.contributor.author Plasencia, Inés
dc.contributor.author Taberner Sanchis, Francisco José
dc.contributor.author Salgado Benito, Jesús
dc.contributor.author Calvete, Juan J.
dc.contributor.author Pérez Gil, Jesús
dc.contributor.author Mingarro Muñoz, Ismael
dc.date.accessioned 2016-11-30T19:13:42Z
dc.date.available 2016-11-30T19:13:42Z
dc.date.issued 2006
dc.identifier.uri http://hdl.handle.net/10550/56214
dc.description.abstract Surfactant protein C (SP-C) is an essential component for the surface tension-lowering activity of the pulmonary surfactant system. It contains a valine-rich α helix that spans the lipid bilayer, and is one of the most hydrophobic proteins known so far. SP-C is also an essential component of various surfactant preparations of animal origin currently used to treat neonatal respiratory distress syndrome (NRDS) in preterm infants. The limited supply of this material and the risk of transmission of infectious agents and immunological reactions have prompted the development of synthetic SP-C-derived peptides or recombinant humanized SP-C for inclusion in new preparations for therapeutic use. We describe herein the recombinant production in bacterial cultures of SP-C variants containing phenylalanines instead of the palmitoylated cysteines of the native protein, as fusions to the hydrophilic nuclease A (SN) from Staphylococcus aureus. The resulting chimerae were partially purified by affinity chromatography and subsequently subjected to protease digestion. The SP-C forms were recovered from the digestion mixtures by organic extraction and further purified by size exclusion chromatography. The two recombinant SP-C variants so obtained retained more than 50% α-helical content and showed surface activity comparable to the native protein, as measured by surface spreading of lipid/protein suspensions and from compression π-A isotherms of lipid/protein films. Compared to the protein purified from porcine lungs, the recombinant SP-C forms improved movement of phospholipid molecules into the interface (during adsorption), or out from the interfacial film (during compression), suggesting new possibilities to develop improved therapeutic preparations.
dc.language.iso eng
dc.relation.ispartof Biochimica et Biophysica Acta-Biomembranes, 2006, vol. 1758, num. 4, p. 509-518
dc.rights.uri info:eu-repo/semantics/openAccess
dc.source Lukovic, Dunja Plasencia, Inés Taberner Sanchis, Francisco José Salgado Benito, Jesús Calvete, Juan J. Pérez Gil, Jesús Mingarro Muñoz, Ismael 2006 Production and characterisation of recombinant forms of human pulmonary surfactant protein C (SP-C): Structure and surface activity Biochimica et Biophysica Acta-Biomembranes 1758 4 509 518
dc.subject Proteïnes de membrana
dc.subject Membranes (Biologia)
dc.subject Bioquímica
dc.title Production and characterisation of recombinant forms of human pulmonary surfactant protein C (SP-C): Structure and surface activity
dc.type info:eu-repo/semantics/article
dc.date.updated 2016-11-30T19:13:42Z
dc.identifier.doi http://dx.doi.org/10.1016/j.bbamem.2006.03.005
dc.identifier.idgrec 033839

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