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Structure Stability and Orientation of BSA Adsorbed to Silica
Mälardalen University, Department of Biology and Chemical Engineering. (Ytbioteknik)
Mälardalen University, Department of Biology and Chemical Engineering. (Ytbioteknik)
Biacore AB, Sweden.
2005 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, Vol. 289, no 1, p. 26-35Article in journal (Other (popular science, discussion, etc.)) 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 nativP structure became fully exposed to the solution.

Place, publisher, year, edition, pages
2005. Vol. 289, no 1, p. 26-35
National Category
Physical Chemistry
Identifiers
URN: urn:nbn:se:mdh:diva-3099DOI: 10.1016/j.jcis.2005.03.064ISI: 000230184200003Scopus ID: 2-s2.0-22044444052OAI: oai:DiVA.org:mdh-3099DiVA, id: diva2:115763
Available from: 2008-03-31 Created: 2008-03-31 Last updated: 2015-07-07Bibliographically approved

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