Biotin Vs Avidin Essay

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which has four binding sites for biotin or biotinylated derivatives with extraordinary affinity. Biotin can be chemically coupled to a binder molecule (e.g., a protein, DNA, hormone, etc.) without disturbing the interaction with its target molecule by a procedure called biotinylation. Avidin can then be exploited to “sandwich” between the biotinylated binder and a targeting molecule or probe. Avidin was also coupled with a functional moiety in some cases. Through the avidin-biotin system, we can achieve various tasks, including localization, identification, assay, etc. (Adams, and Weiner, 2005).
The biotinylation is an essential prerequisite in the successful application of the avidin-biotin technology. It may be accomplished by direct conjugation
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Although ideal for specific labeling, such strong avidin-biotin binding interaction limits the applications of the system in some fields requiring facile capture and release. For example, in theory, avidin or avidin derivatives could be purified by adsorption on an insoluble biotinylated matrix; however, the avidin or avidin derivative is not easily eluted because of such high affinity. The same problems occur for purification of biotin derivatives using the avidin/streptavidin immobilized matrix (Prijovichl, Chen, and Roffler, 2002). For gene delivery using the avidin-biotin system, such high affinity limits viral vector release (Sharma, Bagshawe, and Begent, 2005). Research on the modification of binding in the avidin-biotin system has been reported to increase off-rates and reduce binding …show more content…
The EPR impact brings about the specific sequestration of the remedial proteins in tumors. After organization of prodrugs, the restorative proteins can change over the prodrugs into dangerous structures that execute tumor cells. The viability of this procedure relies on upon upgrading the conveyance of the remedial proteins to the tumor while killing the proteins from the plasma before organization of the prodrug. The upgrade of the plasma half-existence of a PEGylated protein is an imperative essential for EPR focusing on tumor tissues and the span of a PEGylated protein is a pivotal element to keep the PEGylated protein circling in the plasma. It is for the most part suggested that the span of a helpful protein ought to be bigger than the glomerular filtration edge with a specific end goal to abstain from being cleared too rapidly by the renal framework. We trust that a perfect avidin-biotin-PEG-compound complex has a sub-atomic weight higher than the glomerular filtration edge and can build the EPR tumor focusing on. In the meantime, this com plex must separate into avidin and biotin-PEG-CPA in the dissemination framework so it can be

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