Molecular simulation of protein adsorption and conformation at gas-liquid, liquid–liquid and solid–liquid interfaces

Georgios Dalkas, Stephen Robert Euston

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)
66 Downloads (Pure)


The adsorption of proteins at surfaces and interfaces is important in a wide range of industries. Understanding and controlling the conformation of adsorbed proteins at surfaces is critical to stability and function in many technological applications including foods and biomedical testing kits or sensors. Studying adsorbed protein conformation is difficult experimentally and so over the past few decades researchers have turned to computer simulation methods to give information at the atomic level on this important area. In this review we summarize some of the significant simulation work over the past four years at both fluid (liquid-liquid and gas-liquid interfaces) and solid-liquid interfaces. Of particular significance is the work on surfactant proteins such as fungal hydrophobins, ranspumin-2 from the túngara frog and the bacteria protein BslA. These have evolved unique structures impart very high surface-active properties to the molecules. A highlight is the elucidation of the clam-shell unhinging mechanism of ranspumin-2 adsorption to the gas-liquid interface that is responsible for its adsorption to and stabilization of the air bubbles in túngara frog foam nests.
Original languageEnglish
Pages (from-to)1-10
Number of pages10
JournalCurrent Opinion in Colloid and Interface Science
Early online date4 Dec 2018
Publication statusPublished - Jun 2019


  • Fluid interfaces
  • Molecular dynamics
  • Protein adsorption
  • Solid–water interfaces

ASJC Scopus subject areas

  • Surfaces and Interfaces
  • Physical and Theoretical Chemistry
  • Polymers and Plastics
  • Colloid and Surface Chemistry


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