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The formation of pepsin monomolecular layer by the Langmuir–Blodgett film deposition technique

Authors
Journal
Colloids and Surfaces B Biointerfaces
0927-7765
Publisher
Elsevier
Publication Date
Volume
73
Issue
1
Identifiers
DOI: 10.1016/j.colsurfb.2009.05.008
Keywords
  • Pepsin
  • Air/Water Interface
  • Adsorption Kinetics
  • Langmuir–Blodgett Film

Abstract

Abstract We report herein the formation of pepsin monomolecular layer by the Langmuir–Blodgett film deposition technique. An effort was made to find an optimal subphase by adjusting the concentration of salt (KCl) and pH by monitoring the growth kinetics of pepsin for the formation of Langmuir monolayer by using as little as possible pepsin molecules to build up ultra thin film and to measure the extent of denaturation. Significant changes of area/molecule, compressibility, rigidity and unfolding of pepsin are observed at optimized subphase than pure water subphase. Observations at optimal subphase are explained in context of the modified DLVO theory and the site dissociation model. FTIR analysis of amide band together with the observed surface morphology of pepsin film in FE-SEM images indicate that at optimal subphase the pepsin molecules modify their structures by incrementing the β-structure, resulting into larger unfolding and inter-molecular aggregates.

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