Structure and orientation changes of omega- and gamma-gliadins at the air-water interface: A PM-IRRAS Spectroscopy and Brewster angle microscopy study

  • Banc A
  • Desbat B
  • Renard D
 et al. 
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Microscopic and molecular structures of omega- and gamma-gliadin monolayers at the air-water interface were studied under compression by three complementary techniques: compression isotherms, polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS), and Brewster angle microscopy (BAM). For high molecular areas, gliadin films are homogeneous, and a flat orientation of secondary structures relative to the interface is observed. With increasing compression, the nature and orientation of secondary structures changed to minimize the interfacial area. The gamma-gliadin film is the most stable at the air-water interface; its interfacial volume is constant with increasing compression, contrary to omega-gliadin films whose molecules are forced out of the interface. gamma-Gliadin stability at a high level of compression is interpreted by a stacking model.

Author-supplied keywords

  • adsorption
  • alpha-helix
  • central repetitive domain
  • ir spectroscopy
  • optical-constants
  • peptides
  • secondary structures
  • seed-storage proteins
  • transform infrared-spectroscopy
  • wheat gluten proteins

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  • A Banc

  • B Desbat

  • D Renard

  • Y Popineau

  • U Mangavel

  • L Navailles

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