Probing the orientation of surface-immobilized immunoglobulin G by time-of-flight secondary ion mass spectrometry

Static time-of-flight secondary ion mass spectrometry (ToF-SIMS) is a powerful surface analysis technique for the characterization of protein films because of its chemical selectivity and surface sensitivity. In this study, static ToF-SIMS and principal component analysis (PCA), a multivariate data...

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Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 20(2004), 5 vom: 02. März, Seite 1877-87
1. Verfasser: Wang, Hua (VerfasserIn)
Weitere Verfasser: Castner, David G, Ratner, Buddy D, Jiang, Shaoyi
Format: Aufsatz
Sprache:English
Veröffentlicht: 2004
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Antibodies, Monoclonal Gonadotropins Immunoglobulin Fab Fragments Immunoglobulin Fc Fragments Immunoglobulin G
Beschreibung
Zusammenfassung:Static time-of-flight secondary ion mass spectrometry (ToF-SIMS) is a powerful surface analysis technique for the characterization of protein films because of its chemical selectivity and surface sensitivity. In this study, static ToF-SIMS and principal component analysis (PCA), a multivariate data analysis method, were combined to probe the orientation of surface-immobilized immunoglobulin G (IgG). IgG orientation can enhance its ability to detect its antigen in immunoassay techniques. The IgG used in this work is the mouse monoclonal anti-human chorionic gonadotropin (anti-hCG). Anti-hCG films on different well-defined substrates have been studied using its F(ab')2 and Fc fragments as references. Atomic force microscopy was used to characterize these protein films before static ToF-SIMS analysis. The results from PCA of ToF-SIMS spectra were related to the antibody primary amino acid composition and its three-dimensional structure
Beschreibung:Date Completed 29.12.2005
Date Revised 26.10.2019
published: Print
Citation Status MEDLINE
ISSN:1520-5827