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

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.

Complex Micellization Behavior of the Polysorbates Tween 20 and Tween 80

“…For another example, let us consider a liquid formulation of an antibody that contains a surfactant to cover the solution−air and solution−container interfaces in order to avoid the surface-induced denaturation of the protein. 36 For a singlecomponent surfactant, surface coverage would remain unchanged as long as the surfactant concentration remains above the cmc. Within this range, the surfactant concentration can be optimized according to other considerations (viscosity, interactions with other excipients, etc.…”

Characterization of radicals in polysorbate 80 using electron paramagnetic resonance (EPR) spectroscopy and spin trapping

“…On one hand, although little is known about the functionality of specific isolated PS fractions, this variety might be the key to the beneficial and stabilizing properties of PS. On the other hand, the heterogeneity leads to different susceptibilities to degradation of the individual components during storage in pharmaceutical formulations ( Grabarek et al, 2020 ; Khan et al, 2015 ; Rabe et al, 2020 ; Nayem et al, 2020 ).…”

Dependence of the Core–Shell Structure on the Lipid Composition of Nanostructured Lipid Carriers: Implications for Drug Carrier Design

“…These three components were dispersed in an aqueous environment to form the NLC structure (Figure a). Because T80 has a large hydrophilic head group, it is located at the interface and stably disperses particles. , In addition, T80 has an octanol–water partition coefficient (Log P = 4.8) that is less than that of the other components (Figure a, table), implying that T80 is mainly distributed in the region close to the aqueous phase. Our previous study identified the dependence of self-assembly behavior on the NLC composition, including the surfactant concentration .…”