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 organization: Department of Chemistry
Faculty of Agriculture and Forestry
Biosciences
Faculty of Medicine
Laboratory of Analytical Chemistry
Date: 2017
Language: eng
Number of pages: 10
Belongs to series: Analytical Biochemistry
ISSN: 0003-2697
DOI: https://doi.org/10.1016/j.ab.2016.10.024
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
Peer reviewed: Yes
Rights: cc_by_nc_nd
Usage restriction: openAccess
Self-archived version: acceptedVersion


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