Biomolecular recognition

Biomolecular Recognition Is Mediated by Weak Chemical Forces... 

Raschke, G., Kowarik, S., Franzl, T., Sonnichsen, C., Mar, T.A. and Feldmann, J. (2003) Biomolecular recognition based on single gold nanoparticle... 

Main types of biomolecular recognition elements used in affinity biosensors based on spectroscopy of guided modes include antibodies, nucleic acids and biomimetic materials. Antibodies are used most frequently because of their high affinity, versatility, and commercial availability. 

Optical sensors based on spectroscopy of guided waves have been demonstrated for detection and identification of numerous chemical and biological analytes. The choice of detection format for a particular application depends on the size of target analyte molecules, binding characteristics of available biomolecular recognition element, and range of analyte s concentrations to be measured. 

J. A. McCammon, Theory of biomolecular recognition, Curr. Op. Struct. Biol. 8 245... 

This diverse set of biosensing experimental demonstrations illustrates the flexibility of the OFRR device. Nearly any biomolecular recognition event can be detected. The examples illustrated with the previously described experiments include DNA sequence detection and virus detection through surface proteins. Additional biosensing examples for which the OFRR is well-suited include site-specific cleavage, protein-protein interactions, and cell genotype/phenotype identification through receptors. Furthermore, as shown by the theory outlined above, the OFRR can be accurately and precisely quantitative. 

CNTs can be functionalized with protein via non-covalent bond (Li et al., 2005 Kim et al., 2003 Mitchell et al., 2002). For example, (beta-lactamase I, that can be immobilized inside or outside CNTs, doesn t change enzyme s activity (Vinuesa and Goodnow, 2002). Taq enzyme can attach to the outside of CNT, and doesn t change its activity (Cui et al., 2004). Peptide with Histidine and Tryptophan can have selective affinity for CNT(Guo et al., 1998). Monoclonal antibody can attach to SWNTs. Protein-modified CNTs can be used to improve its biocompatibility and biomolecular recognition capabilities (Um et al., 2006). For example, CNTs functionalized with PEG and Triton X-100 can prevent nonspecific binding of protein and CNTs. Biotin moiety is attached to the PEG chains Streptavidin can bind specifically with biotin-CNT (Shim et al., 2002). 

Shim M, Kam NMS, Chen RJ, Li R, Dai H (2002). Lunctionalization of carbon nanotubes for biocompatibility and biomolecular recognition. Nano Lett. 2 285-288. 

Jelesarov, I. and H.R. Bosshard. 1999. Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J Mol Recognit 12 3-18. 

SPR biosensors are label-free detection devices - binding between the biomolecular recognition element and analyte can be observed directly without the use of radioactive or fluorescent labels. In addition, the binding event can be observed in real-time. SPR affinity biosensors can, in principle, detect any analyte for which an appropriate biomolecular recognition element is available. Moreover, analyte molecules do not have to exhibit any special properties such as fluorescence or characteristic absorption or scattering bands. 

An SPR biosensor consists of two key elements - an optical system for excitation and interrogation of surface plasmons and a biospecific coating incorporating biomolecular recognition elements which interact with target molecules in a sample. 

Various types of biomolecular recognition elements have been exploited in affinity biosensors. These include antibodies ", aptamers, peptides , and... 

Colton, I.J., Carbeck, J.D., Rao, J., Whitesides, G.M. Affinity capillary electrophoresis a physical-organic tool for studying interactions in biomolecular recognition. Electrophoresis 1998, 19, 369-382. 

Y-H Chu, CC Cheng. Affinity capillary electrophoresis in biomolecular recognition. Cell Mol Life Sci 54 663-683, 1998. 

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