Publicacions

• Membrane-bound structure and alignment of antimicrobial β-sheet peptide gramicidin S derived from angular and distance constraints by solid state 19F-NMR

  Salgado, J.; Grage, S. L.; Kondejewski, L. H.; Hodges, R.; McElhaney, R. N.; Ulrich, A. S.

  (2001).Article

  J. Biomol. NMR.

  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...

  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.

  Llegir mésOcultar

  21: 191-208

  DOI: 10.1016/j.bbamem.2006.03.005

• The closed/open model for lipase activation. Addressing intermediate active forms of fungal enzymes by trapping of conformers in water-restricted environments.

  González-Navarro, H.; Bañó, M. C.; Abad, C.

  (2001).Article

  Biochemistry.

  40: 3174-3183

• Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane

  Nilsson, I.; Witt, S.; Kiefer, H.; Mingarro, I.; von Heijne, G.

  (2000).Article

  J. Biol. Chem..

  275: 6207-6213

• Influence of the C-terminus of Glycophorin A transmembrane fragment on the dimerization process

  Orzáez, M.; Pérez-Payá, E.; Mingarro, I.

  (2000).Article

  Protein Sci..

  9: 1246-53

• Identification of peptides that neutalize bacterial endotoxins using β-hairpin conformationally restricted libraries

  González-Navarro, H.; Mora, P.; Pastor, M.; Serrano, L.; Mingarro, I.; Pérez-Payá, E.

  (2000).Article

  Mol. Divers..

  5: 117-27

• Different conformations of nascent polypeptides during translocation across the ER membrane

  Mingarro, I.; Nilsson, I. M.; Whitley. P.; von Heijne, G.

  (2000).Article

  BMC Cell Biology.

  1: 1-8