dc.contributorUniversidade Federal de São Paulo (UNIFESP)
dc.creatorCaseli, Luciano [UNIFESP]
dc.creatorCavalheiro, Renan Pelluzzi [UNIFESP]
dc.creatorNader, Helena Bonciani [UNIFESP]
dc.creatorLopes, Carla Cristina [UNIFESP]
dc.date.accessioned2016-01-24T14:27:08Z
dc.date.accessioned2023-09-04T18:33:55Z
dc.date.available2016-01-24T14:27:08Z
dc.date.available2023-09-04T18:33:55Z
dc.date.created2016-01-24T14:27:08Z
dc.date.issued2012-05-01
dc.identifierBiochimica Et Biophysica Acta-biomembranes. Amsterdam: Elsevier B.V., v. 1818, n. 5, p. 1211-1217, 2012.
dc.identifier0005-2736
dc.identifierhttp://repositorio.unifesp.br/handle/11600/34810
dc.identifierWOS000302971100011.pdf
dc.identifier10.1016/j.bbamem.2012.01.012
dc.identifierWOS:000302971100011
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8616229
dc.description.abstractInvestigating the role of proteoglycans associated to cell membranes is fundamental to comprehend biochemical process that occurs at the level of membrane surfaces. in this paper, we exploit syndecan-4, a heparan sulfate proteoglycan obtained from cell cultures, in lipid Langmuir monolayers at the air-water interface. the monolayer served as a model for half a membrane, and the molecular interactions involved could be evaluated with tensiometry and vibrational spectroscopy techniques. Polarization-modulation infrared reflection-absorption spectroscopy (PM-IRRAS) employed in a constant surface pressure regime showed that the main chemical groups for syndecan-4 were present at the air-water interface. Subsequent monolayer decompression and compression showed surface pressure-area isotherms with a large expansion for the lipid monolayers interacting with the cell culture reported to over-express syndecan-4, which was also an indication that the proteoglycan was inserted in the lipid monolayer. the introduction of biological molecules with affinity for syndecam-4, such as growth factors, which present a key role in biochemical process of cell signaling, changed the surface properties of the hybrid film, leading to a model, by which the growth factor binds to the sulfate groups present in the heparan sulfate chains. the polypeptide moiety of syndecan-4 responds to this interaction changing its conformation, which leads to lipid film relaxation and further monolayer condensation. (C) 2012 Elsevier B.V. All rights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationBiochimica Et Biophysica Acta-biomembranes
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.rightsAcesso aberto
dc.subjectHeparan sulfate proteoglycan
dc.subjectSyndecan-4
dc.subjectMolecular recognizing
dc.subjectLangmuir monolayer
dc.titleProbing the interaction between heparan sulfate proteoglycan with biologically relevant molecules in mimetic models for cell membranes: A Langmuir film study
dc.typeArtigo


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