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- Title
Cost-effective downstream processing of recombinantly produced pexiganan peptide and its antimicrobial activity.
- Authors
Sun, Baode; Wibowo, David; Middelberg, Anton P. J.; Zhao, Chun-Xia
- Abstract
Antimicrobial peptides (AMPs) have significant potential as alternatives to classical antibiotics. However, AMPs are currently prepared using processes which are often laborious, expensive and of low-yield, thus hindering their research and application. Large-scale methods for production of AMPs using a cost-effective approach is urgently required. In this study, we report a scalable, chromatography-free downstream processing method for producing an antimicrobial peptide, pexiganan, using recombinant Escherichia coli ( E. coli). The four helix bundle structure of the unique carrier protein DAMP4 was used to facilitate a simple and cheap purification process based on a selective thermochemical precipitation. Highly pure fusion protein DAMP4-pexiganan was obtained at high yield (around 24 mg per 800 mL cell culture with a final cultivation OD ~ 2). The purification yield of DAMP4-pexiganan protein is increased twofold with a 72.9% of the protein recovery in this study as compared to the previous purification processes (Dwyer in Chem Eng Sci 105:12-21, 2014). The antimicrobial peptide pexiganan was released and activated from the fusion protein by a simple acid-cleavage. Isoelectric precipitation was then applied to separate the pexiganan peptide from the DAMP4 protein carrier. The final yield of pure bio-produced pexiganan was 1.6 mg from 800 mL of bacterial cell culture (final cultivation OD ~ 2). The minimum bactericidal concentration (MBC) test demonstrated that the bio-produced pexiganan has the same antimicrobial activity as chemically synthesized counterpart. This novel downstream process provides a new strategy for simple and probable economic production of antimicrobial peptides.
- Subjects
PEPTIDE drugs; GENETIC recombination; ANTI-infective agents; COST effectiveness; CELL culture; CHROMATOGRAPHIC analysis; BACTERIA
- Publication
AMB Express, 2018, Vol 8, Issue 1, p1
- ISSN
2191-0855
- Publication type
Article
- DOI
10.1186/s13568-018-0541-3