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Three complementary techniques for the clarification of temperature effect on low-density lipoprotein–chondroitin-6-sulfate interaction
Laboratory of Analytical Chemistry, Department of Chemistry, University of Helsinki.
Laboratory of Analytical Chemistry, Department of Chemistry, University of Helsinki.
Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper.ORCID-id: 0000-0003-1819-1709
Wihuri Research Institute, FIN-00290 Helsinki, Finland.
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2013 (engelsk)Inngår i: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 443, nr 2, s. 139-147Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Abstract A rigorous processing of adsorption data from quartz crystal microbalance technology was successfully combined with the data obtained by partial filling affinity capillary electrophoresis and molecular dynamics for the clarification of the temperature effect on the interaction of a major glycosaminoglycan chain chondroitin-6-sulfate (C6S) of proteoglycans with low-density lipoprotein (LDL) and with a peptide fragment of apolipoprotein B-100 (residues 3359–3377 of LDL, PPBS). Two experimental techniques and computational atomistic methods demonstrated a nonlinear pattern of the affinity of C6S at temperatures above 38.0 °C to both LDL and PPBS. The temperature affects the interaction of C6S with LDL and PPBS by influencing the structural behavior of glycosaminoglycan C6S and/or that of LDL.

sted, utgiver, år, opplag, sider
2013. Vol. 443, nr 2, s. 139-147
Emneord [en]
Adsorption energy distribution, Glycosaminoglycan, Low-density lipoprotein, Molecular dynamics simulations, Partial filling affinity capillary electrophoresis, Quartz crystal microbalance
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Forskningsprogram
Kemi
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URN: urn:nbn:se:kau:diva-30221DOI: 10.1016/j.ab.2013.09.014ISI: 000327279700004PubMedID: 24055620OAI: oai:DiVA.org:kau-30221DiVA, id: diva2:667165
Tilgjengelig fra: 2013-11-25 Laget: 2013-11-25 Sist oppdatert: 2019-07-12bibliografisk kontrollert

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