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ToF-SIMS and PCA of surface-immobilized antibodies with different orientations

Authors
Park, Ji-WonCho, Il-HoonMoon, Dae WonPaek, Se-HwanLee, Tae Geol
Issue Date
1월-2011
Publisher
WILEY
Keywords
ToF-SIMS; principal component analysis; antibody; orientation
Citation
SURFACE AND INTERFACE ANALYSIS, v.43, no.1-2, pp.285 - 289
Indexed
SCIE
SCOPUS
Journal Title
SURFACE AND INTERFACE ANALYSIS
Volume
43
Number
1-2
Start Page
285
End Page
289
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/113429
DOI
10.1002/sia.3440
ISSN
0142-2421
Abstract
A number of studies have been done on the orientation of surface-immobilized antibodies since it plays a significant role in the performance of immunoassays. Here, we present a new study by which the orientation of differently immobilized antibodies was directly probed by using time-of-flight secondary ion mass spectrometry (ToF-SIMS) and principal component analysis (PCA). For greater control over the orientations of intact IgG and F(ab')(2) antibody fragment, they were either site-directly biotinylated at the hinge region or randomly biotinylated at the amino groups, and were then immobilized onto a streptavidin-terminated surface. According to the PCA results from ToF-SIMS spectra, site-directly and randomly biotinylated IgG became 'end-on' oriented (Fc is closer to the surface) at a gradual rate as immobilization concentration increased, while site-directly biotinylated IgG became oriented at a slightly faster rate. Furthermore, site-directly biotinylated F(ab')(2) quickly became 'end-on' oriented even at a low concentration of 1 mu g/ml as immobilization concentration increased, whereas randomly biotinylated F(ab')(2) was not oriented at all over any concentration. Our results show that a ToF-SIMS partnership with multivariate analysis is useful for interpreting protein orientations in terms of surface amino acid profiles. Copyright (C) 2010 John Wiley & Sons, Ltd.
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