This title appears in the Scientific Report :
2018
Please use the identifier:
http://hdl.handle.net/2128/21068 in citations.
Understanding Microscale Thermophoresis: contributions by simple building blocks of proteins
Understanding Microscale Thermophoresis: contributions by simple building blocks of proteins
Understanding Microscale Thermophoresis:Contributions by simple building blocks of proteinsM.Bjelcic, D. Niether1 and S.Wiegand1;21ICS-3 Soft Condensed Matter, Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany2Department für Chemie - Physikalische Chemie, Universität zu Köln, 50939 Cologne,Germ...
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Personal Name(s): | Bjelcic, Monika (Corresponding author) |
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Niether, Doreen / Dhont, Jan K.G. / Wiegand, Simone | |
Contributing Institute: |
Weiche Materie; ICS-3 |
Imprint: |
2018
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Conference: | Jülich Soft Matter Days, Jülich (Germany), 2018-11-20 - 2018-11-23 |
Document Type: |
Poster |
Research Program: |
Functional Macromolecules and Complexes |
Link: |
OpenAccess OpenAccess |
Publikationsportal JuSER |
Understanding Microscale Thermophoresis:Contributions by simple building blocks of proteinsM.Bjelcic, D. Niether1 and S.Wiegand1;21ICS-3 Soft Condensed Matter, Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany2Department für Chemie - Physikalische Chemie, Universität zu Köln, 50939 Cologne,GermanyE-mail: s.wiegand@fz-juelich.deIn recent years Microscale Thermophoresis (MST), an analytical approach to monitor proteinligandbinding reactions, gained a lot of interest [1]. This method needs less sample comparedto calorimetric methods and is therefore very useful for pharmaceutical applications. Even forsimple molecules the underlying microscopic processes are not understood. The situation iseven more complicated in the case of proteins. Depending on their folding state they behaveas charged rigid colloids or more flexible polymers. When conformational changes modify theratio of hydrophilic and hydrophobic side groups in contact with water, this influences the hydrationlayer. There is a superb sensitivity of the thermophoretic behaviour of the protein due tothese local rearrangements of water molecules. Recent experiments for various amides showeda clear correlation of the temperature dependence of the Soret coefficient with the hydrophilicity[2], quantitatively described by the logarithm of the 1-octanol/water partition coefficient P.This coefficient is a measure for the hydrophilicity/hydrophobicity balance of a solute and isoften used to model the transport of a compound in the environment or to screen for potentialpharmaceutical compounds. It could be shown that the concept works also for sugars, nonsteroidalanti-inflammatory drugs and cyclodextrins [3]. As it is known that also the ionic strengthand charges have a strong influence on the observed thermophoretic behavior [4], we investigatesystematically various aqueous solutions of alcohols and amino acids with varying hydrophobicity,polarity and charge of the side groups. As experimental method we use a holographicgrating technique called infrared Thermal Diffusion Forced Rayleigh Scattering (IR-TDFRS).References[1] M. Jerabek-Willemsen, T. Andre, R. Wanner, H. M. Roth, S. Duhr, P. Baaske and D.Breitsprecher, J. Mol. Struct., 1077, 101-113, (2014)[2] D. Niether, H. Kriegs, J. K. G. Dhont and S.Wiegand, J. Chem. Phy., (2018) under review[3] D. Niether, T. Kawaguchi, J. Hovancova, K. Eguchi, J. K. G. Dhont, R. Kita and S. Wiegand,Langmuir 33, 8483-8492, (2017)[4] H. Ning, J. K. G. Dhont and S. Wiegand, Langmuir, 24, 2426-2432, (2008) |