dc.contributor.author | Fernández Higuero, José Ángel | |
dc.contributor.author | Salvador, Ana M. | |
dc.contributor.author | Martín Plágaro, César Augusto | |
dc.contributor.author | González Milicua, José Carlos | |
dc.contributor.author | Rodríguez Arrondo, José Luis | |
dc.date.accessioned | 2016-02-02T10:17:28Z | |
dc.date.available | 2016-02-02T10:17:28Z | |
dc.date.issued | 2014-03-18 | |
dc.identifier.citation | PLOS ONE 9(3) : (2014) // Article ID e92426 | es |
dc.identifier.issn | 1932-6203 | |
dc.identifier.uri | http://hdl.handle.net/10810/17173 | |
dc.description.abstract | Lipoproteins are responsible for cholesterol traffic in humans. Low density lipoprotein (LDL) delivers cholesterol from liver to peripheral tissues. A misleading delivery can lead to the formation of atherosclerotic plaques. LDL has a single protein, apoB-100, that binds to a specific receptor. It is known that the failure associated with a deficient protein-receptor binding leads to plaque formation. ApoB-100 is a large single lipid-associated polypeptide difficulting the study of its structure. IR spectroscopy is a technique suitable to follow the different conformational changes produced in apoB-100 because it is not affected by the size of the protein or the turbidity of the sample. We have analyzed LDL spectra of different individuals and shown that, even if there are not big structural changes, a different pattern in the intensity of the band located around 1617 cm 21 related with strands embedded in the lipid monolayer, can be associated with a different conformational rearrangement that could affect to a protein interacting region with the receptor. | es |
dc.description.sponsorship | This work has been supported in part by MINECO grant (BFU 2006-14423) and Programa INNPACTO (grant NuIPT-2011-0817-010000). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. No additional funding received for this study. | es |
dc.language.iso | eng | es |
dc.publisher | Public Library Science | es |
dc.relation | info:eu-repo/grantAgreement/MINECO/BFU 2006-14423 | |
dc.rights | info:eu-repo/semantics/openAccess | es |
dc.subject | low-density-lipoprotein | es |
dc.subject | coronary-heart-disease | es |
dc.subject | transform infrared-spectroscopy | es |
dc.subject | defective apolipoprotein B100 | es |
dc.subject | plasma-lipoproteins | es |
dc.subject | secondary structure | es |
dc.subject | risk-factor | es |
dc.subject | particle | es |
dc.subject | cholesterol | es |
dc.subject | receptor | es |
dc.title | Human LDL Structural Diversity Studied by IR Spectroscopy | es |
dc.type | info:eu-repo/semantics/article | es |
dc.rights.holder | © 2014 Fernéndez-Higuero et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. | es |
dc.relation.publisherversion | http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0092426#abstract0 | es |
dc.identifier.doi | 10.1371/journal.pone.0092426 | |
dc.departamentoes | Bioquímica y biología molecular | es_ES |
dc.departamentoeu | Biokimika eta biologia molekularra | es_ES |
dc.subject.categoria | AGRICULTURAL AND BIOLOGICAL SCIENCES | |
dc.subject.categoria | MEDICINE | |
dc.subject.categoria | BIOCHEMISTRY AND MOLECULAR BIOLOGY | |