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Structure, stability, and orientation of BSA adsorbed to silica
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology.
2005 (English)In: Journal of Colloid and Interface Science, Vol. Available on-line April 18, 2005Article in journal (Refereed) Published
Abstract [en]

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
Keyword [en]
adsorption, BSA, DSC, protein, proteolysis, mass spectrometry, silica
Identifiers
URN: urn:nbn:se:uu:diva-70225OAI: oai:DiVA.org:uu-70225DiVA: diva2:98136
Available from: 2005-05-31 Created: 2005-05-31 Last updated: 2011-01-12

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