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Figure | (A) Code sun. A protein's blueprint is the DNA which is translated into mRNA and later a peptide chain. (B) Illustration of the Peptide Bond. Depicted is a generic tetrapeptide of unspecified residues.

"As an essential component of the cell, bioactive peptides and proteins are as natural as they can be."

Peptides and Proteins

Most of the organic compounds of living cells belong to one of four classes of molecules, i.e. carbohydrates, lipids, peptides and proteins, or nucleic acids (in alphapetical order). Thereby, according to the central dogma of molecular biology, information flows the direction from DNA to RNA (transcription) and from RNA to protein (translation).
It is the peptides and proteins that are tasked to fulfill and maintain the molecular function and biological processes of the cells, respectively. Proteins are build from a combination of 21 natural amino acids, their biological activity and function are determined by composition, sequence as well as secondary and terrtierry structure. The number of possible peptides and proteins is virtually limitless and, as an essential component of the cell, bioactive peptides and proteins are as natural as they can be.

"The problem? The availability! is the availability of cost-effective and affordable and clean peptide ."

BEtter Peptides Platform for Tailor-Made Linear and circular Peptides and Proteins

Functional bioactive peptides and proteins have an enormous but underutilised economical potential to improve the ecological balance in several major industry sectors producing or processing biological material.
, for instance, the agriculture, food, pharma or cosmetic sector.
For example, antimicrobial peptides can protect sensitive crop and/or temporarily prepare them naturally for climate change-related environmental impacts, such as droughts and pests, without the disadvantages of risking formation of resistence, hazardous residues and drift into adjacent soils or groundwater. Furthermore, in the production of vegan meat, the availability of protein-based growth factors plays a crucial role, and as flavour modulators, peptides can significantly reduce added sugars.
The problem? The availability!

Patents and Patent applications

BPP GmbH has filed several patent application (see below) describing its revolutionary innovative biotechnological process for the production of complex linear and cyclic peptides and small proteins (15 - 250 amino acids in size). Key features of the technology are that the process can produce any conceivable peptide sequence without production-related residues of relative high purity (> 95%) while being scalable up to the scale of tons. The complete elimination of highly specialised chemicals and the simplicity of product preparation further reduce production costs, which ultimately determine the economic viability of using peptide-based alternatives in agriculture and the food industry.

  1. PCT/EP2019/050892: Biotechnological production of tailor-made peptides
  2. US: patent granted (Patent number US 11,697,809 B2)
  3. Eurasia: patent granted (Patent number 202091713)  
  4. PCT/EP2021/060892: pH-switch optimized smart release fusion protein for peptide production (Patent pending)
  5. PCT/EP2023/053466: Biotechnological production of cyclic peptide classes (Patent pending)
  6. EP22183641: Peptide-based transfection/transformation agents (Patent pending)

"Our well engineered multi-functional designer fusion protein comes with (almost) all molecular tools needed to clean itself."

The Better Peptides Platform - I: The Fusion protein

The basis of our Better Peptides Platform is a well engineered, multi-functional, and patented designer fusion protein for expression, protection, isolation, purification, and on-demand release of tailor-made linear and circular peptides. In other words, the BPP fusion protein comes with (almost) all molecular tools needed to clean itself.

Briefly, the BPP fusion protein consists of three noteworthy domains:
First, the Carrier & Binding (CB) Domain has a strong tendency to agglomerate in inclusion bodies when expressed in bacterial cultures (see advantages below). In addition, it exhibits a natural affinity to readily available and inexpensive biological purification matrixes allowing it to be purified in high yields (> 95%) using simple, reliable, and scalable chromatography processes. No hazardous solvents required!
Second, our Smart Release (SR) Domain (patent pending) exhibits an optimized pH-sensitive proteolytic activity that represents a well controlled release trigger of the final product. Most importantly, it releases the target linear or cyclic peptide or protein with authentic termini, i.e. there are no process related amino acid residues or elimination reactions.
Lastly, there is the Payload (P). The payload is your custom linear or cyclic peptides of 20 - 250 amino acid length. The possibilities are virtually limitless.

You already have a linear or cyclic peptide candidate that you would like to move into a flexible and scalable production pipeline? The Better Peptides Platform is probably the answer. Please contact us and we work together on a solution for your production needs.
In addition, we have a few promising peptide and protein candidates of our own, ready to be taken into culture and to be produced on demand.

Figure | Stock Photo of our Founder (Placeholder)

Figure | SDS Page Bubbles (Placeholder)

"By producing the peptide and protein precursors in inclusion bodies, we let the host cell work for us - not against us."

The Better Peptides Platform - II: Production in Bacterial Inclusion bodies

Inclusion bodies are semi-crystalline aggregates or granules of presumably unfunctional and misfolded protein residing inside bacterial cells. Recombinantly expressed genes are often not optimized for the host cellular enviroment and are regarded a major stress factor or even potentially harmful for the host cells when exhibiting an enzymatical activity. As a response, the bacterial host compartmentalizes recombinant proteins to protect itself from the protein load and/or abberant non-native functions. In fact, between 70% and 80% of recombinant proteins expressed E. coli are contained in inclusion bodies.

The Better Peptides Platform takes advantage of the natural tendency of certain recombinant proteins to be contained in inclusion bodies providing natural protection from degradation, increased stability, easy purification/separation as well as high yields from semi-crystalline structures.