Thermodynamic and kinetic approaches for evaluation of monoclonal antibody - Lipoprotein interactions

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Multia , E , Sirén , H , Andersson , K , Samuelsson , J , Forssén , P , Fornstedt , T , Öörni , K , Jauhiainen , M & Riekkola , M-L 2017 , ' Thermodynamic and kinetic approaches for evaluation of monoclonal antibody - Lipoprotein interactions ' , Analytical Biochemistry , vol. 518 , pp. 25-34 . https://doi.org/10.1016/j.ab.2016.10.024

Title: Thermodynamic and kinetic approaches for evaluation of monoclonal antibody - Lipoprotein interactions
Author: Multia, Evgen; Sirén, Heli; Andersson, Karl; Samuelsson, Jörgen; Forssén, Patrik; Fornstedt, Torgny; Öörni, Katariina; Jauhiainen, Matti; Riekkola, Marja-Liisa
Contributor: University of Helsinki, Department of Chemistry
University of Helsinki, Faculty of Agriculture and Forestry
University of Helsinki, Biosciences
University of Helsinki, Faculty of Medicine
University of Helsinki, Department of Chemistry
Date: 2017
Language: eng
Number of pages: 10
Belongs to series: Analytical Biochemistry
ISSN: 0003-2697
URI: http://hdl.handle.net/10138/307958
Abstract: Two complementary instrumental techniques were used, and the data generated was processed with advanced numerical tools to investigate the interactions between anti-human apoB-100 monoclonal antibody (anti-apoB-100 Mab) and apoB-100 containing lipoproteins. Partial Filling Affinity Capillary Electrophoresis (PF-ACE) combined with Adsorption Energy Distribution (AED) calculations provided information on the heterogeneity of the interactions without any a priori model assumptions. The AED calculations evidenced a homogenous binding site distribution for the interactions. Quartz Crystal Microbalance (QCM) studies were used to evaluate thermodynamics and kinetics of the Low-Density Lipoprotein (LDL) and anti-apoB-100 Mab interactions. High affinity and selectivity were observed, and the emerging data sets were analysed with so called Interaction Maps. In thermodynamic studies, the interaction between LDL and anti-apoB-100 Mab was found to be predominantly enthalpy driven. Both techniques were also used to study antibody interactions with Intermediate-Density (IDL) and Very Low Density (VLDL) Lipoproteins. By screening affinity constants for IDL-VLDL sample in a single injection we were able to distinguish affinity constants for both subpopulations using the numerical Interaction Map tool. (C) 2016 Elsevier Inc. All rights reserved.
Subject: Monoclonal anti-apoB-100 antibody
Lipoproteins
Thermodynamics
Kinetics
Interaction map
AFFINITY CAPILLARY-ELECTROPHORESIS
QUARTZ-CRYSTAL MICROBALANCE
ENERGY-DISTRIBUTION CALCULATIONS
LOW-DENSITY-LIPOPROTEIN
CLARIFICATION
DISTRIBUTIONS
ELUCIDATION
PARTICLES
SERUM
116 Chemical sciences
1182 Biochemistry, cell and molecular biology
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