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Design and Application of Autofluorescent Proteins by Biological Incorporation of Intrinsically Fluorescent Noncanonical Amino Acids
Citation key 140.2016.durkin
Author Durkin, P. M. and Budisa, N.
Title of Book Fluorescent Analogs of Biomolecular Building Blocks -Design and Applications
Pages 91 – 124
Year 2016
ISBN 978-1-118-17586-6
Editor Marcus Wilhelmsson (Editor), Yitzhak Tor (Editor)
Publisher Wiley
Chapter 5
Abstract Traditional use of autofluorescent proteins in biology, biotechnology and medicine is becoming increasingly useful in synthetic biological applications as both: (i) the reporters of enzyme catalyzed chemical transformation as well as (ii) noninvasive encoders of individual protein(s) in the complex cellular environments. The majority of protein chromophores are either generated intrinsically during protein maturation or are attached post-translationally. On the other hand, the use of canonical aromatic amino acids building blocks as optical probes is limited. However, this can be circumvented by the chemical functionalization of their side chains with a wide variety of organic frameworks and subsequent genetic encoding. In this chapter, we focus on the chemical synthetic efforts to create fluorescent amino acids having small organic fluorophores such as indole analogs, as well as biological methodologies to incorporate them directly (by expanded genetic code) into the target protein scaffolds. Now, with the availability of the orthogonal pairs in the protein biosynthesis many optical applications can rely on the use of biologically accessible intrinsic chromophores with an “amino acid format” as a rational approach for direct design of new auto-fluorescent proteins. For example, chemical diversification of indole side chain makes accessible a great diversity of molecular structures encompassing a wide range of interesting electronic systems. Proteins synthesized in this way are endowed with unique photophysical properties such as absorbance, quantum yield, Stokes shift, lifetime and the ability to respond changes in the environment, intrinsic protein structure or physiological status.
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