An albumin-derived peptide scaffold capable of binding and catalysis
| Autor: | Elisa Maurizio, Riccardo Sgarra, Alessandro Tossi, Immacolata Luisi, Adriano Savoini, Giampaolo Fontanive, Silvia Pavan, Federico Berti, Fabio Benedetti, Daniele Sblattero |
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| Přispěvatelé: | Luisi, Immacolata, Pavan, Silvia, Fontanive, Giampaolo, Tossi, Alessandro, Benedetti, Fabio, Savoini, A., Maurizio, Elisa, Sgarra, Riccardo, Sblattero, Daniele, Berti, Federico |
| Rok vydání: | 2012 |
| Předmět: |
biorecognition
lcsh:Medicine Sequence (biology) Peptide Plasma protein binding Biochemistry peptide scaffords Macromolecular Structure Analysis General Materials Science Biomacromolecule-Ligand Interactions Amino Acids lcsh:Science Glutathione Transferase chemistry.chemical_classification Multidisciplinary biology Chemistry albumin biocatalysis Amino acid Organic Acids peptide scafford Codon usage bias Protein Binding Research Article Biotechnology Protein Structure Stereochemistry Recombinant Fusion Proteins Serum albumin Catalysis Albumins Chemical Biology Humans Binding site Protein Interactions Biology Serum Albumin Diketone lcsh:R Organic Chemistry Tryptophan Proteins Computational Biology Fusion protein biology.protein Biocatalysis lcsh:Q Peptides Cysteine |
| Zdroj: | PLoS ONE PLoS ONE, Vol 8, Iss 2, p e56469 (2013) Nature Precedings |
| ISSN: | 1932-6203 |
| Popis: | We have identified a 101-amino-acid polypeptide derived from the sequence surrounding the IIA binding site of human albumin. The polypeptide contains residues that make contact with ligands as warfarin in the parent protein, and eight cysteine residues to form disulfide bridges, which stabilize the polypeptide structure. Seventy-four amino acids are located in six [alpha]-helical regions, with the remaining amino acids forming six connecting coil/loop regions. Codon usage optimization was used to express a GST fusion protein in E. coli in yields as high as 4 mg/l. This fusion protein retains its structural integrity and aldolase activity, the ability to direct the stereochemical outcome of a diketone reduction, and its binding capacity to warfarin and efavirenz. Notably, this newly cloned polypeptide represents a valuable starting point for the construction of libraries of binders and catalysts with improved proficiency. |
| Databáze: | OpenAIRE |
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