Data/hora: 02/06/2024 09:39:45

Provedor de dados: | 17
País: | United Kingdom
Título: | An albumin-derived peptide scaffold capable of binding and catalysis
Autores: | Immacolata Luisi; Silvia Pavan; Giampaolo Fontanive; Alessandro Tossi; Fabio Benedetti; Adriano Savoini; Elisa Maurizio; Riccardo Sgarra; Daniele Sblattero; Federico Berti.
Data: | 2012-02-17
Ano: | 2012
Palavras-chave: | Biotechnology; Chemistry.
Resumo: | 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.
Tipo: | Manuscript

Identificador:

http://precedings.nature.com/documents/6894/version/1

oai:nature.com:10101/npre.2012.6894.1

http://hdl.handle.net/10101/npre.2012.6894.1

Fonte: | Nature Precedings
Fonte: | Creative Commons Attribution 3.0 License