Surface tension measurement and calculation of model biomolecular condensates

Jack Holland, Alfonso A. Castrejón-Pita, Remco Tuinier, Dirk G.A.L. Aarts (Corresponding author), Timothy J. Nott (Corresponding author)

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2 Citaten (Scopus)
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The surface tension of liquid-like protein-rich biomolecular condensates is an emerging physical principle governing the mesoscopic interior organisation of biological cells. In this study, we present a method to evaluate the surface tension of model biomolecular condensates, through straighforward sessile drop measurements of capillary lengths and condensate densities. Our approach bypasses the need for characterizing condensate viscosities, which was required in previously reported techniques. We demonstrate this method using model condensates comprising two mutants of the intrinsically disordered protein Ddx4N. Notably, we uncover a detrimental impact of increased protein net charge on the surface tension of Ddx4N condensates. Furthermore, we explore the application of Scheutjens-Fleer theory, calculating condensate surface tensions through a self-consistent mean-field framework using Flory-Huggins interaction parameters. This relatively simple theory provides semi-quantitative accuracy in predicting Ddx4N condensate surface tensions and enables the evaluation of molecular organisation at condensate surfaces. Our findings shed light on the molecular details of fluid-fluid interfaces in biomolecular condensates.

Originele taal-2Engels
Pagina's (van-tot)8706-8716
Aantal pagina's11
TijdschriftSoft Matter
Nummer van het tijdschrift45
StatusGepubliceerd - 7 dec. 2023

Bibliografische nota

Publisher Copyright:
© 2023 The Royal Society of Chemistry.


J. H. thanks Mark Vis for introducing them to Scheutjens–Fleer theory. Also thanks to Clare Rees-Zimmerman and Callum Beck for providing helpful comments during the writing process. J. H. acknowledges the Synthetic Biology Centre for Doctoral Training – EPSRC funding (EP/L016494/1) and Christ Church, Oxford, for funding. T. J. N. acknowledges the Wellcome Trust and the Royal Society (Grant Number 202320/Z/16/Z) for funding. A. A. C. P. gratefully acknowledges funding support from the NSF/CBET-EPSRC via grant No. EP/W016036/1.

Synthetic Biology Centre for Doctoral Training
Wellcome Trust Sanger Institute
Engineering and Physical Sciences Research CouncilEP/L016494/1
Royal Society202320/Z/16/Z
Neurosciences Foundation


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