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Study on orientation of immunoglobulin G on protein G layer.
Biosens Bioelectron. 2005 Jul 15; 21(1):103-10.BB

Abstract

A comparative study of immunoglobulin G (IgG) immobilization was performed, both on a thiolated protein G layer, where this immobilization was due to affinity binding with an Fc fragment of IgG, and on 11-mercaptoundecanoic acid (11-MUA), where the immobilization was due to chemical bonding. The change of IgG layer formation on the two base layers as a function of the IgG concentration was investigated by surface plasmon resonance (SPR), atomic force microscopy (AFM) in a non-contact mode, and spectroscopic ellipsometry (SE). It was observed that the IgG layer was immobilized more evenly on the thiolated protein G layer than on the 11-MUA layer, based on the SPR measurements. The surface topology analysis by AFM indicated that the IgG layer was immobilized on the protein G layer according to the envelope profile of the base layer. Based on the SE analysis, it was determined that the IgG layer thickness on the thiolated protein G layer increased with increasing IgG concentration. Based on the above analyses, the scheme for orientation of IgG immobilized on the thiolated protein G layer was proposed.

Authors+Show Affiliations

Bae YM
Department of Chemical and Biomolecular Engineering, Sogang University, 1 Sinsu-Dong, Mapo-Gu, Seoul 121-742, South Korea.
Oh BK
No affiliation info available
Lee W
No affiliation info available
Lee WH
No affiliation info available
Choi JW
No affiliation info available

MeSH

Biosensing TechniquesGoldImmunoglobulin GMicroscopy, Atomic ForceNerve Tissue ProteinsSulfhydryl CompoundsSurface Plasmon Resonance

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15967357

Citation

Bae, Young Min, et al. "Study On Orientation of Immunoglobulin G On Protein G Layer." Biosensors & Bioelectronics, vol. 21, no. 1, 2005, pp. 103-10.
Bae YM, Oh BK, Lee W, et al. Study on orientation of immunoglobulin G on protein G layer. Biosens Bioelectron. 2005;21(1):103-10.
Bae, Y. M., Oh, B. K., Lee, W., Lee, W. H., & Choi, J. W. (2005). Study on orientation of immunoglobulin G on protein G layer. Biosensors & Bioelectronics, 21(1), 103-10.
Bae YM, et al. Study On Orientation of Immunoglobulin G On Protein G Layer. Biosens Bioelectron. 2005 Jul 15;21(1):103-10. PubMed PMID: 15967357.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Study on orientation of immunoglobulin G on protein G layer. AU - Bae,Young Min, AU - Oh,Byung-Keun, AU - Lee,Woochang, AU - Lee,Won Hong, AU - Choi,Jeong-Woo, PY - 2004/07/02/received PY - 2004/08/30/revised PY - 2004/09/03/accepted PY - 2005/6/22/pubmed PY - 2008/3/6/medline PY - 2005/6/22/entrez SP - 103 EP - 10 JF - Biosensors & bioelectronics JO - Biosens Bioelectron VL - 21 IS - 1 N2 - A comparative study of immunoglobulin G (IgG) immobilization was performed, both on a thiolated protein G layer, where this immobilization was due to affinity binding with an Fc fragment of IgG, and on 11-mercaptoundecanoic acid (11-MUA), where the immobilization was due to chemical bonding. The change of IgG layer formation on the two base layers as a function of the IgG concentration was investigated by surface plasmon resonance (SPR), atomic force microscopy (AFM) in a non-contact mode, and spectroscopic ellipsometry (SE). It was observed that the IgG layer was immobilized more evenly on the thiolated protein G layer than on the 11-MUA layer, based on the SPR measurements. The surface topology analysis by AFM indicated that the IgG layer was immobilized on the protein G layer according to the envelope profile of the base layer. Based on the SE analysis, it was determined that the IgG layer thickness on the thiolated protein G layer increased with increasing IgG concentration. Based on the above analyses, the scheme for orientation of IgG immobilized on the thiolated protein G layer was proposed. SN - 0956-5663 UR - https://www.unboundmedicine.com/medline/citation/15967357/Study_on_orientation_of_immunoglobulin_G_on_protein_G_layer_ DB - PRIME DP - Unbound Medicine ER -