Correlation between mechanical behavior of protein films at the air/water interface and intrinsic stability of protein molecules

A.H. Martin, M.A. Cohen Stuart, M.A. Bos, T. van Vliet

Research output: Contribution to journalArticleAcademicpeer-review

43 Citations (Scopus)


The relation between mechanical film properties of various adsorbed protein layers at the air/water interface and intrinsic stability of the corresponding proteins is discussed. Mechanical film properties were determined by surface deformation in shear and dilation. In shear, fracture stress, ¿f, and fracture strain, ¿f, were determined, as well as the relaxation behavior after macroscopic fracture. The dilatational measurements were performed in a Langmuir trough equipped with an infra-red reflection absorption spectroscopy (IRRAS) accessory. During compression and relaxation of the surface, the surface pressure, ¿, and adsorbed amount, ¿ (determined from the IRRAS spectra), were determined simultaneously. In addition, IRRAS spectra revealed information on conformational changes in terms of secondary structure. Possible correlations between macroscopic film properties and intrinsic stability of the proteins were determined and discussed in terms of molecular dimensions of single proteins and interfacial protein films. Molecular properties involved the area per protein molecule at ¿ ¿ 0 mN/m (A0), A0/M (M = molecular weight) and the maximum slope of the ¿-¿ curves (d¿/d¿). The differences observed in mechanical properties and relaxation behavior indicate that the behavior of a protein film subjected to large deformation may vary widely from predominantly viscous (yielding) to more elastic (fracture). This transition is also observed in gradual changes in A0/M. It appeared that in general protein layers with high A 0/M have a high ¿f and behave more fluidlike, whereas solidlike behavior is characterized by low A0/M and low ¿f. Additionally, proteins with a low A0/M value have a low adaptability in changing their conformation upon adsorption at the air/water interface. Both results support the conclusion that the hardness (internal cohesion) of protein molecules determines predominantly the mechanical behavior of adsorbed protein layers
Original languageEnglish
Pages (from-to)4083-4089
Issue number9
Publication statusPublished - 2005


  • air-water-interface
  • surface rheological properties
  • liquid interfaces
  • conformational aspects
  • beta-lactoglobulin
  • shear rheology
  • adsorption
  • layers
  • ovalbumin
  • reflection

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