Evaluation and biosynthetic incorporation of chlorotyrosine into recombinant proteins

Recently, non-canonical amino acids (NCAA) incorporation was developed to enhance the functional properties of proteins. Incorporation of NCAA containing chlorine atom is conceptually an attractive approach to prepare pharmacologically active substances, which is a difficult task since chlorine is b...

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Bibliographic Details
Published in:Biotechnology and bioprocess engineering 2012, 17(4), , pp.679-686
Main Authors: Ayyadurai, Niraikulam, King Saud University, Riyadh, Saudi Arabia, Deepankumar, Kanagavel, Yeungnam University, Gyeongsan, Republic of Korea, Prabhu, Nadarajan Saravanan, Yeungnam University, Gyeongsan, Republic of Korea, Budisa, Nediljko, Biocatalysis Group, Institute of Chemistry, Berlin Institute of Technology/TU Berlin, Berlin, Germany, Yun, H.D., Yeungnam University, Gyeongsan, Republic of Korea
Format: Article
Language:English
Subjects:
Amino acids
Analysis
Binding sites
Bioinformatics
Biotechnology
Chemical engineering
Chemistry
Chemistry and Materials Science
Chlorine
chloro-tyrosine
E coli
Efficiency
Genetic engineering
GFP
homology modeling
Industrial and Production Engineering
noncanonical amino acids
Polymers
protein engineering
Protein folding
Protein synthesis
PROTEINAS
PROTEINE
PROTEINS
Research Paper
Studies
Transfer RNA
Translation
Tyrosine
생물공학
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Summary:Recently, non-canonical amino acids (NCAA) incorporation was developed to enhance the functional properties of proteins. Incorporation of NCAA containing chlorine atom is conceptually an attractive approach to prepare pharmacologically active substances, which is a difficult task since chlorine is bulky atom. In this study, we evaluated the efficiency and extent of in vivo incorporation of tyrosine analogue 3-chlorotyrosine [(3-Cl)Tyr] into the recombinant proteins GFP and GFPHS (highly stable GFP). The incorporation of (3-Cl)Tyr into GFP leads to dramatic reduction in the expression level of protein. On the other hand, the incorporation of (3-Cl)Tyr into GFPHS was expressed well as a soluble form. In addition we used bioinformatics tools for the analysis to explore the possible constraints in micro-environment of each natural amino acid residue to be replaced with chlorine atom accommodation into GFPHS. In conclusion, our approaches are reliable and straightforward way to enhance the translation of chlorinated amino acids into proteins.
ISSN:1226-8372
1976-3816
DOI:10.1007/s12257-012-0066-6