NAGIOS: RODERIC FUNCIONANDO

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

Repositori DSpace/Manakin

IMPORTANT: Aquest repositori està en una versió antiga des del 3/12/2023. La nova instal.lació está en https://roderic.uv.es/

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

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.citation	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.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.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	journal article	es_ES
dc.date.updated	2016-11-30T19:13:42Z
dc.identifier.doi	10.1016/j.bbamem.2006.03.005
dc.identifier.idgrec	033839
dc.rights.accessRights	open access	es_ES