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mk2 Biotechnologies: Combination in protein production

mk2 Biotechnologies develops, produces and studies complex proteins with diverse chemical and physical proteries and the highest degree of purity. These services are complemented by consulting and screening services in order to analyze, for example, an extended peptide family regarding its impact on different pathogenes. Using a scalable disruptvie method, mk2 Biotechnologies is able to synthesize complex peptides authentically and at low cost.

The team at mk2 Biotechnologies is convinced that incremental improvements will not be able to meet today's and even less tomorrow's challenges. Overcoming the hurdles of the next 100 years that might not even be known today requires new, radical ideas and revolutionary technologies. The whole team of mk2 Biotechnologies has strong confidende in the proprietary disruptive technology, the products and applications. It is motivated by the tremenous potential of this technology to reduce big societal problems or even solve them using sustainably produced biobased products. In the long term, crop production products with unwanted side effects, antibiotics and active ingredients in cosmetics and pharmaceuticals could be replaced by peptides, providing a large value to general health.

The recombinant synthesis process developed by mk2 Biotechnologies is based on a well-established method for protein synthesis (>> 100 amino acids) where the target molecule is produced by reproductive genetically modified bacteria. For short-chain peptides the principle so far could not be applied as the small peptides could not be separated efficiently from bacteria or bacterial debris. Thus it has not been possible to produce high purity peptides with authentic amino acid sequences and termini at competitive cost. Especially the non-scalable purification step (mostly by HPLC) created an enormous bottleneck. 

Coupling of fusion protein and column resin

The mk2 Biotechnologies process is a highly innovative advanced development based on existing recombinant processes. The major innovation in the process is the combination of the fusion protein with the resin used in the purification column that renders additional purification, e.g. by costly non-scalable HPLC technologies obsolete. This innovation is complemented by an interface in the fusion prtein that allows for controlled release of the target peptide independent of its composition or length.

The technical simplicity of the process enables a scalable and thus cost-efficient synthesis of any authentic peptide at highest puritiy. Neither chemical (length or repetitive sequences) nor physical (polarity or charge) properties are a barrier to synthesis. The disruptive process allows for the environmentally friendly production of peptides on an industrial scale.