Expression of acid cleavable Asp-Pro linked multimeric AFP peptide in E. coli

Background Difficult to express peptides are usually produced by co-expression with fusion partners. In this case, a significant mass part of the recombinant product falls on the subsequently removed fusion partner. On the other hand, multimerization of peptides is known to improve its proteolytic s...

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Veröffentlicht in:	Journal of Genetic Engineering and Biotechnology 2021-10, Vol.19 (1), p.155-10, Article 155
Hauptverfasser:	Mollaev, Murad, Zabolotskii, Artur, Gorokhovets, Neonila, Nikolskaya, Elena, Sokol, Maria, Tsedilin, Andrey, Mollaeva, Mariia, Chirkina, Margarita, Kuvaev, Timofey, Pshenichnikova, Anna, Yabbarov, Nikita
Format:	Artikel
Sprache:	eng
Schlagworte:	acid hydrolysis Alpha-fetoprotein Asp-Pro cleavage Aspartate Biomedical Engineering and Bioengineering biotechnology Cytotoxicity Design optimization Drug delivery Drug delivery systems Drugs E coli Engineering enzymatic hydrolysis Enzymes Escherichia coli Formic acid Fusion protein Glycoproteins High-performance liquid chromatography humans Hydrolysis Liver cancer Molecular weight Multimer expression Peptides Plasmids Proline Proteolysis Reagents Recombinant peptide recombinant peptides Solid phase methods Solid phase synthesis Stability Vehicles α-Fetoprotein
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