Scientific Reports (Jan 2024)

Kinetic study of membrane protein interactions: from three to two dimensions

  • Vladimir Adrien,
  • Myriam Reffay,
  • Nicolas Taulier,
  • Alice Verchère,
  • Laura Monlezun,
  • Martin Picard,
  • Arnaud Ducruix,
  • Isabelle Broutin,
  • Frédéric Pincet,
  • Wladimir Urbach

DOI
https://doi.org/10.1038/s41598-023-50827-5
Journal volume & issue
Vol. 14, no. 1
pp. 1 – 10

Abstract

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Abstract Molecular interactions are contingent upon the system’s dimensionality. Notably, comprehending the impact of dimensionality on protein–protein interactions holds paramount importance in foreseeing protein behaviour across diverse scenarios, encompassing both solution and membrane environments. Here, we unravel interactions among membrane proteins across various dimensionalities by quantifying their binding rates through fluorescence recovery experiments. Our findings are presented through the examination of two protein systems: streptavidin–biotin and a protein complex constituting a bacterial efflux pump. We present here an original approach for gauging a two-dimensional binding constant between membrane proteins embedded in two opposite membranes. The quotient of protein binding rates in solution and on the membrane represents a metric denoting the exploration distance of the interacting sites—a novel interpretation.