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Exploring of protein – protein interactions at the solid – aqueous interface by means of contact angle measurements.pdf

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Exploring of protein – protein interactions at the solid – aqueous interface by means of contact angle measurements.pdf

Colloids and Surfaces B: Biointerfaces 141 (2016) 558–564 Contents lists available at ScienceDirect Colloids and Surfaces B: Biointerfaces journal homepage: /locate/colsurfb Exploring of protein – protein interactions at the solid – aqueous interface by means of contact angle measurements I. Grabowska a,?, W. Dehaen b, H. Radecka a, J. Radecki a a Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, Tuwima 10, 10-748 Olsztyn, Poland b Department of Chemistry, KU Leuven, Celestijnenlaan 200F, B-3001 Leuven, Belgium article info Article history: Received 21 August 2015 Received in revised form 15 January 2016 Accepted 2 February 2016 Available online 4 February 2016 Keywords: Cu(II) or Ni(II) complexes with dipyrromethene (DPM) Histidine-tagged VC1 domain of Receptor for Advanced Glycation End Products (RAGE) RAGE interactions with S100B Contact angle measurements Acid-base interfacial properties abstract In this article we present the results of the studies on interactions between the VC1 domain of the Receptor for Advanced Glycation End Products (RAGE) and its ligand, the S100B protein, performed by contact angle measurements. Histidine-tagged (His6) VC1-RAGE domain was covalently bonded to Cu(II) or Ni(II) complexes with dipyrromethene (DPM) self-assembled on gold surface. The method based on the theory of van Oss was used for the purpose of determining the Lifshitz–van der Waals (?LW) component as well as the electron acceptor—electron donor (the Lewis acid–base, ?+–??) parameters of the VC1RAGE-S100B complex. Moreover, the surface free energies of the interactions between the VC1 domain attached to the surface and the ligand present in the aqueous phase were determined. The speci?city of the VC1- RAGE interactions with the ligand studied was also proved. ? 2016 Elsevier B.V. All rights reserved. 1. Introduction The immobilization of proteins on solid substrates has recently attracted much attention [1–3]. Many studies are related to the