The penetration of melittin and myelin basic protein into glycosphingolipid monolayers depends on the lipid polar head group, the protein concentration available and the initial surface pressure. The lipid-protein interaction leads to modification of the surface properties of both the glycosphingolipid and the proteins.
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http://dx.doi.org/10.1042/bj1930643 | DOI Listing |
J Phys Chem B
November 2015
Department of Chemistry and Biochemistry, Wilfrid Laurier University , 75 University Ave. W., Waterloo, Ontario, Canada N2L 3C5.
Model membranes composed of various lipid mixtures can segregate into liquid-ordered (Lo) and liquid-disordered (Ld) phases. In this study, lipid vesicles composed of mainly Lo or Ld phases as well as complex lipid systems representing the cytosolic leaflet of the myelin membrane were characterized by fluorescence resonance energy transfer with a donor/acceptor pair that preferentially partitioned into Lo or Ld phases, respectively. The fluidity of the lipid systems containing >30% cholesterol was modulated in the presence of the amphipathic peptide melittin.
View Article and Find Full Text PDFIran J Pharm Res
November 2013
Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran.
Multiple sclerosis (MS) is a progressive and autoimmune neurodegenerative disease of the central nervous system (CNS). This disease is recognized through symptoms like inflammation, demyelination and the destruction of neurological actions. Experimental allergic encephalomyelitis (EAE) is a widely accepted animal model for MS.
View Article and Find Full Text PDFJ Appl Physiol (1985)
May 2009
Div. of Pulmonary Biology, Cincinnati Children's Hospital Medical Center, ML #7029, 3333 Burnet Ave., Cincinnati, Ohio 45229-3039, USA.
Surfactant protein (SP)-D plays an important role in host defense and pulmonary surfactant homeostasis. In SP-D-deficient (Sftpd(-/-)) mice, the abnormal large surfactant forms seen at the ultrastructural level are taken up inefficiently by type II cells, resulting in an over threefold increase in the surfactant pool size. The mechanisms by which SP-D influences surfactant ultrastructure are unknown.
View Article and Find Full Text PDFBiochem J
May 2004
UMR 5546 CNRS/Université Paul Sabatier, Pôle de Biotechnologie Végétale, BP 17 Auzeville, 31326 Castanet-Tolosan cedex, France.
Screening a cDNA expression library with a radiolabelled calmodulin (CaM) probe led to the isolation of AtCaMRLK, a receptor-like kinase (RLK) of Arabidopsis thaliana. AtCaMRLK polypeptide sequence shows a modular organization consisting of the four distinctive domains characteristic of receptor kinases: an amino terminal signal sequence, a domain containing seven leucine-rich repeats, a single putative membrane-spanning segment and a protein kinase domain. Using truncated versions of the protein and a synthetic peptide, we demonstrated that a region of 23 amino acids, located near the kinase domain of AtCaMRLK, binds CaM in a calcium-dependent manner.
View Article and Find Full Text PDFBiochim Biophys Acta
November 1998
Biomembrane Structure Unit, Biochemistry Department, Oxford University, Oxford OX1 3QU, UK.
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