Structure, stability, and orientation of BSA adsorbed to silica
2005 (English)In: Journal of Colloid and Interface Science, Vol. Available on-line April 18, 2005Article in journal (Refereed) Published
In this investigation, the structure, stability, and orientation of bovine serum albumin (BSA) adsorbed onto silica particles were studied
using differential scanning calorimetry (DSC) and limited proteolysis in combination with mass spectrometry (MS). DSC gave information
on the overall structural stability of BSA while limited proteolysis was used to probe the accessibility of enzymatic cleavage sites, thereby
yielding information on the orientation and structure of BSA adsorbed to silica surfaces. Thermal investigation of BSA in various buffers,
both free in solution and in the adsorbed state, showed that solutes that surround the protein played an important role with respect to the
overall structural stability and the structural heterogeneity of BSA. Limited proteolysis with trypsin and chymotrypsin indicated that BSA in
the adsorbed state is oriented with domain 2 facing the silica surface. Also, upon adsorption, no additional cleavage sites were exposed. The
combination of the results presented in this study implied that BSA molecules adsorbed onto silica particles were significantly reduced in
their structural stability, but not to an extent that internal residues within the native structure became fully exposed to the solution.
2005 Elsevier Inc. All rights reserved.
Place, publisher, year, edition, pages
2005. Vol. Available on-line April 18, 2005
adsorption, BSA, DSC, protein, proteolysis, mass spectrometry, silica
IdentifiersURN: urn:nbn:se:uu:diva-70225OAI: oai:DiVA.org:uu-70225DiVA: diva2:98136