DOI | Resolve DOI: https://doi.org/10.1016/j.bioorg.2006.12.004 |
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Author | Search for: Noestheden, Matthew1; Search for: Hu, Qingyan1; Search for: Tay, Li-Lin2; Search for: Tonary, Angela M.1; Search for: Stolow, Albert1; Search for: MacKenzie, Roger3; Search for: Tanha, Jamshid3; Search for: Pezacki, John Paul1 |
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Affiliation | - National Research Council of Canada. NRC Steacie Institute for Molecular Sciences
- National Research Council of Canada. NRC Institute for Microstructural Sciences
- National Research Council of Canada. NRC Institute for Biological Sciences
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Format | Text, Article |
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Subject | Antigen-Antibody Reactions; Benzoic Acids; Molecular Structure; Protein Structure, Tertiary; Sensitivity and Specificity; Serum Albumin, Bovine; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrum Analysis, Raman; Staphylococcal Protein A; Staphylococcus aureus; Structure-Activity Relationship; Succinimides; Surface Plasmon Resonance; Vibration |
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Abstract | A recombinant VH single-domain antibody recognizing staphylococcal protein A was functionalized on reactive lysine residues with N-hydroxysuccimidyl-activated 4-cyanobenzoate. Surface plasmon resonance analysis of antibody-antigen binding revealed that modified and unmodified antibodies bound protein A with similar affinities. Raman imaging of the modified antibodies indicated that the benzonitrile group provides vibrational contrast enhancement in a region of the electromagnetic spectrum that is transparent to cellular materials. Thus, the modified single-domain antibody may be amenable to detecting protein A from samples of the human pathogen Staphylococcus aureus using vibronic detection schemes such as Raman and coherent anti-Stokes Raman scattering. The generality of this labeling strategy should make it applicable to modifying an array of proteins with varied structure and function. |
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Publication date | 2007-06 |
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In | |
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Language | English |
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Peer reviewed | Yes |
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NPARC number | 12327431 |
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Export citation | Export as RIS |
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Report a correction | Report a correction (opens in a new tab) |
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Record identifier | 87e5f5e7-ef0c-4969-a865-c6bbb6b2c6fc |
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Record created | 2009-09-10 |
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Record modified | 2020-05-10 |
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