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  Albumin displacement at the air-water interface by Tween (Polysorbate) surfactants

Rabe, M., Kerth, A., Blume, A., & Garidel, P. (2020). Albumin displacement at the air-water interface by Tween (Polysorbate) surfactants. European Biophysics Journal with Biophysics Letters. doi:10.1007/s00249-020-01459-4.

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Rabe2020_Article_AlbuminDisplacementAtTheAirWat.pdf (Supplementary material), 8MB
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 Creators:
Rabe, Martin1, Author              
Kerth, Andreas2, Author              
Blume, Alfred2, Author              
Garidel, Patrick3, Author              
Affiliations:
1Interface Spectroscopy, Interface Chemistry and Surface Engineering, Max-Planck-Institut für Eisenforschung GmbH, Max Planck Society, ou_1863358              
2Institute of Chemistry, Physical Chemistry, Martin-Luther-University Halle-Wittenberg, von-Danckelmann-Platz 4, 06120, Halle/Saale, Germany, ou_persistent22              
3Boehringer Ingelheim Pharma GmbH and Co. KG, Innovation Unit, PDB, 88397, Biberach an der Riss, Germany, ou_persistent22              

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Free keywords: REFLECTION-ABSORPTION SPECTROSCOPY; BETA-CASEIN LAYERS; AIR/WATER INTERFACE; AIR/SOLUTION INTERFACE; OROGENIC DISPLACEMENT; PROTEIN FORMULATIONS; SERUM ALBUMINS; ADSORPTION; BINDING; MICROSCOPYBiophysics; Protein; Albumin; Tween (polysorbate); IRRAS; BAM; Protein-surfactant interaction;
 Abstract: Tween (polysorbate) 20 and 80 are surfactants used for the development of parenteral protein drugs, due to their beneficial safety profile and stabilisation properties. To elucidate the mechanism by which Tween 20 and 80 stabilise proteins in aqueous solutions, either by a "direct" protein to surfactant interaction and/or by an interaction with the protein film at the air-water interface, we used spectroscopic (Infrared Reflection Absorption Spectroscopy, IRRAS) and microscopic techniques (Brewster Angle Microscopy, BAM) in combination with surface pressure measurements. To this end, the impact of both types of Tweens with regard to the displacement of the protein from the air-water interface was studied. As a model protein, human serum albumin (HSA) was used. The results for the displacement of the adsorbed HSA films by Tweens 20 and 80 can partially be understood on the basis of an orogenic displacement mechanism, which depends on the critical surface pressure of the adsorbed protein film. With increasing concentration of Tween in the sub-phase, BAM images showed the formation of different domain morphologies. IRRA-spectra supported the finding that at high protein concentration in the sub-phase, the protein film could not be completely displaced by the surfactants. Comparing the impact of both surfactants, we found that Tween 20 adsorbed faster to the protein film than Tween 80. The adsorption kinetics of both Tweens and the speed of protein displacement increased with rising surfactant concentration. Tween 80 reached significant lower surface pressures than Tween 20, which led to an incomplete displacement of the observed HSA film.

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Language(s): eng - English
 Dates: 2020-09-11
 Publication Status: Published in print
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/s00249-020-01459-4
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Title: European Biophysics Journal with Biophysics Letters
  Other : European Biophysics Journal with Biophysics Letters
Source Genre: Journal
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Publ. Info: Berlin : Springer
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: ISSN: 0175-7571
CoNE: https://pure.mpg.de/cone/journals/resource/954925487773