Synthesis and characterization of CN-modified protein analogues as potential vibrational contrast agents

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DOIResolve DOI: http://doi.org/10.1016/j.bioorg.2006.12.004
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TypeArticle
Journal titleBioorg. Chem
Bioorganic Chemistry
ISSN0045-2068
Volume35
Issue3
Pages28493; # of pages: 192
SubjectAntigen-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
AbstractA 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.
Publication date
AffiliationNational Research Council Canada; NRC Institute for Microstructural Sciences; NRC Steacie Institute for Molecular Sciences; NRC Institute for Biological Sciences
Peer reviewedNo
Identifier10056087
NPARC number12327431
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Record identifier87e5f5e7-ef0c-4969-a865-c6bbb6b2c6fc
Record created2009-09-10
Record modified2016-05-09
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