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TM-AFM Threshold Analysis of Macromolecular Orientation: A Study of the Orientation of IgG and IgE on Mica Surfaces
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology.
1998 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 206, no 2, 475-481 p.Article in journal (Refereed) Published
Abstract [en]

Adsorption and orientation properties of two different types of immunoglobulin molecules on derivatized and native mica surfaces were investigated using TM-AFM. The analyses included height measurements at two different pH values and a new technique, presented here as threshold analysis, which displays the outer mantle shape of an adsorbed protein. A major difference in preferential orientation is observed upon comparing the adsorption of the two proteins onto the different surfaces. The characteristics of both the adsorbed immunoglobulin and the surface are important for any preferential orientation of the adsorbed protein.

Place, publisher, year, edition, pages
1998. Vol. 206, no 2, 475-481 p.
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:uu:diva-89709DOI: 10.1006/jcis.1998.5630Scopus ID: 9756659OAI: oai:DiVA.org:uu-89709DiVA: diva2:161413
Available from: 2002-03-19 Created: 2002-03-19 Last updated: 2013-05-30Bibliographically approved
In thesis
1. Orientation and Conformation of Single Macromolecules on Unmodified and Functionalized Surfaces
Open this publication in new window or tab >>Orientation and Conformation of Single Macromolecules on Unmodified and Functionalized Surfaces
2002 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

In this thesis methods for investigation of orientation and conformation of individual macromolecules on surfaces are presented as well as novel methods for functionalization of silicon chips with the possibility to get an ordered immobilization of antibodies.

Two novel methods are presented which makes it possible to investigate the orientation of individual macromolecules on different kinds of surfaces with AFM. One is based on threshold patterning where, depending on substrate, side- and end-on adsorbed immunoglobulin molecules could be detected. The other method is using the principle of site-specific ligands where the orientation of proteins adsorbed to various surfaces was evaluated. By measuring the increase in protein volume of the formed protein-ligand complexes with AFM, the amount of protein having an orientation that allows binding can be estimated.

The influence of surface chemistry on protein structure was examined using human serum fibronectin adsorbed to hydrophilic and hydrophobic surfaces, where a major difference in structure were seen depending on surface properties.

In addition, methods for surface functionalization have been developed which are suitable for immobilization of macromolecules and for basic studies of macromolecule/surface interactions at the nanometer scale. In an effort to immobilize protein in a specific orientation that could be studied with AFM, a new method for preparing reactive disulfides based upon a mixed reaction with 2,2’-dipyridyldisulfide and 2-thiopyridone to a mercapto-silanized silica surface was presented. The possibility to covalently bind proteins to this surface was examined, using beta-galactosidase and Fab’-fragments of IgG.

Place, publisher, year, edition, pages
Uppsala: Acta Universitatis Upsaliensis, 2002. 62 p.
Series
Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, ISSN 1104-232X ; 694
Keyword
Biotechnology, Atomic Force Microscopy, protein orientation, protein adsorption, surface derivatization, Bioteknik
National Category
Industrial Biotechnology
Research subject
Surface Biotechnology
Identifiers
urn:nbn:se:uu:diva-1854 (URN)91-554-5259-0 (ISBN)
Public defence
2002-04-11, B41, Uppsala, 14:00
Opponent
Available from: 2002-03-19 Created: 2002-03-19Bibliographically approved

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