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Recombinant antimicrobial peptides efficiently produced using novel cloning and purification processes
Author(s) -
Metlitskaia Luba,
Cabralda Jennifer E.,
Suleman Dinar,
Kerry Cynthia,
Brinkman Jacquelyn,
Bartfeld Daniel,
Guarna M. Marta
Publication year - 2004
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba20030100
Subject(s) - escherichia coli , antimicrobial , antimicrobial peptides , recombinant dna , peptide , inclusion bodies , biochemistry , fusion protein , biology , amphiphile , chemistry , microbiology and biotechnology , organic chemistry , gene , copolymer , polymer
Endogenous antimicrobial peptides are ubiquitous components of animal and plant host defences. These peptides, usually cationic and amphipathic, kill target cells rapidly and are efficacious against antibiotic‐resistant and clinically relevant pathogens. A practical challenge in the development of cationic peptides as therapeutics is to meet the production requirements for large quantities of highly purified drug substance at competitive costs. While chemical peptide synthesis can be used to manufacture cationic peptides, we have developed cost‐effective methods for recombinant production by expressing fusion proteins comprised of multiple copies of the peptides. The fusion proteins accumulate in Escherichia coli inclusion bodies and constitute over 50% of the total cellular proteins. Active antimicrobial peptides are released by chemical reagents and purified by chromatography, combining both standard and novel approaches. Challenges of industrial‐scale manufacturing of therapeutics were considered in the development of this process.