Three complementary techniques for the clarification of temperature effect on low-density lipoprotein-chondroitin-6-sulfate interaction.
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.
Laboratory of Analytical Chemistry, Department of Chemistry, University of Helsinki, FIN-00014 Helsinki, Finland. Electronic address: geraldine.cilpa@helsinki.fi.
Geraldine
G
Cilpa-Karhu
Katriina
K
Lipponen
Jörgen
J
Samuelsson
Katariina
K
Oörni
Torgny
T
Fornstedt
Marja-Liisa
ML
Riekkola
D002809:Chondroitin Sulfates / Q000737:chemistry / Q000378:metabolism*; D019075:Electrophoresis, Capillary; D006801:Humans; D008077:Lipoproteins, LDL / Q000737:chemistry / Q000378:metabolism*; D056004:Molecular Dynamics Simulation; D058525:Quartz Crystal Microbalance Techniques; D013696:Temperature
D008077:Lipoproteins, LDL; D002809:Chondroitin Sulfates
Adsorption energy distribution; Glycosaminoglycan; Low-density lipoprotein; Molecular dynamics simulations; Partial filling affinity capillary electrophoresis; Quartz crystal microbalance