Human insulin adsorption kinetics, conformational changes and amyloidal aggregate formation on hydrophobic surfaces
| Autor: | Bhagyashree Jain, Marianne Weidenhaupt, Franz Bruckert, Perry Guo, Yves Bréchet, Laurent Nault |
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| Přispěvatelé: | Science et Ingénierie des Matériaux et Procédés (SIMaP), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Institut de Chimie du CNRS (INC)-Institut National Polytechnique de Grenoble (INPG), Laboratoire des matériaux et du génie physique (LMGP ), Institut National Polytechnique de Grenoble (INPG)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2013 |
| Předmět: |
Amyloid
Conformational change Time Factors Surface Properties medicine.medical_treatment Kinetics Biomedical Engineering Infrared spectroscopy Protein aggregation 010402 general chemistry 01 natural sciences Biochemistry Biomaterials 03 medical and health sciences Adsorption Spectroscopy Fourier Transform Infrared Monolayer medicine Humans Insulin Surface plasmon resonance Protein Structure Quaternary Molecular Biology 030304 developmental biology 0303 health sciences Chemistry [CHIM.MATE]Chemical Sciences/Material chemistry General Medicine Surface Plasmon Resonance 0104 chemical sciences Crystallography Calibration Hydrophobic and Hydrophilic Interactions Biotechnology |
| Zdroj: | Acta Biomaterialia Acta Biomaterialia, Elsevier, 2013, 9 (2), pp.5070-5079. ⟨10.1016/j.actbio.2012.09.025⟩ |
| ISSN: | 1742-7061 |
| Popis: | International audience; The formation of insulin amyloidal aggregates on material surfaces is a well-known phenomenon with important pharmaceutical and medical implications. Using surface plasmon resonance imaging, we monitor insulin adsorption on model hydrophobic surfaces in real time. Insulin adsorbs in two phases: first, a very fast phase (less than 1 min), where a protein monolayer forms, followed by a slower one that can last for at least I h, where multilayered protein aggregates are present. The dissociation kinetics reveals the presence of two insulin populations that slowly interconvert: a rapidly dissociating pool and a pool of strongly bound insulin aggregates. After I h of contact between the protein solution and the surface, the adsorbed insulin has practically stopped dissociating from the surface. The conformation of adsorbed insulin is probed by attenuated total reflection-Fourier transform infrared spectroscopy. Characteristic shifts in the amide A and amide II' bands are associated with insulin adsorption. The amide I band is also distinct from that of soluble or aggregated insulin, and it slowly evolves in time. A 1708 cm(-1) peak is observed, which characterizes insulin adsorbed for times longer than 30 min. Finally, Thioflavin T, a marker of extended beta-sheet structures present in amyloid fibers, binds to adsorbed insulin after 30-40 min. Altogether, these results reveal that the conformational change induced in insulin upon binding to hydrophobic surfaces allows further insulin binding from the solution. Adsorbed insulin is thus an intermediate along the alpha-to-beta structural transition that results in the formation of amyloidal fibers on these material surfaces. (C) 2012 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved. |
| Databáze: | OpenAIRE |
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