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

Bioorganic chemistry (2007-02-24)
Matthew Noestheden, Qingyan Hu, Li-Lin Tay, Angela M Tonary, Albert Stolow, Roger MacKenzie, Jamshid Tanha, John Paul Pezacki
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
4-Cyanobenzoic acid, 99%