10
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: not found
      • Article: not found

      Dissimilar pH-dependent adsorption features of bovine serum albumin and α-chymotrypsin on mica probed by AFM

      , , ,
      Colloids and Surfaces B: Biointerfaces
      Elsevier BV

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          We studied bovine serum albumin (BSA) and alpha-chymotrypsin adsorption onto mica surfaces over a large pH range by atomic force microscopy (AFM) measurements in liquid. Data analyses (height, roughness and roughness factor) brought new insights on the conformation of proteins in soil environments, with mica as a model of soil phyllosilicates and non-hydrophobic surfaces. Validation of AFM approach was performed on BSA, whose behavior was previously described by nuclear magnetic resonance and infra-red spectroscopic methods. Maximum adsorption was observed near the isoelectric point (IEP). A stronger interaction and a lower amount of adsorbed proteins were observed below the IEP, which contrasted with the progressive decrease of adsorption above the IEP. We then studied the adsorption of alpha-chymotrypsin, a proteolytic enzyme commonly found in soils. AFM pictures demonstrated a complete coverage of the mica surface at the IEP in contrast to the BSA case. Comparison of the AFM data with other indirect methods broadened the understanding of alpha-chymotrypsin adsorption process through the direct display of the protein adsorption patterns as a function of pH.

          Related collections

          Author and article information

          Journal
          Colloids and Surfaces B: Biointerfaces
          Colloids and Surfaces B: Biointerfaces
          Elsevier BV
          09277765
          May 2009
          May 2009
          : 70
          : 2
          : 226-231
          Article
          10.1016/j.colsurfb.2008.12.036
          19186036
          258d1540-9aa3-459a-95ee-03b5d65bfd5c
          © 2009

          https://www.elsevier.com/tdm/userlicense/1.0/


          Comments

          Comment on this article