Pharmacist  in aisle of Pharmacy

Proteomimetic Peptide Platform

Biopolymers governing the functions of life include peptides, proteins, RNA and DNA. They consist of α-amino acids and nucleotides. Nature has developed a high diversity of proteins for different functions, such as enzymes, receptors, transport proteins, etc. In order to carry out their roles, they need to fold into well-defined hierarchical 3D structures.


Proteomimetic peptidic constructs are non-natural self-organizing biomimicking systems. They exhibit similar properties to those of proteins, e.g. they have a tendency to fold into specific periodic compact structures with given biomedical function.

Proteomimetic peptidic constructs have the potential to achieve structural versatility similar to that of the natural proteins, and consequently they have numerous promising biological applications where the tailored 3D structure is crucial. Such peptidic constructs based on appropriate structural features and pharmaceutical applications can be designated protein mimics, thus they are a novel class of drug scaffolds with tailored molecular shape and surface.


We developed a novel and highly efficient technology to synthesize such proteomimetic peptides and their derivatives. The methodology allows the application of only 1.5 equivalents of amino acids during coupling, while maintaining quantitative conversions. The continuous-flow meso-scale reactor allows the application of high temperature and pressure during the synthesis.


The complete characterization of the peptidic construct is routinely performed in our state of the art facilities equipped with LD/CD spectrophotometer, NMR spectrometers, custom-made SAXS, WAXS instruments, FF-TEM, SFG spectroscopy, spectrofluorimeter and  HPLC.

Aerial View of Curved Road


Nature has established various molecular architectures to rapidly create proteins with large functional variety. However, sometimes the machinery fails, and the natural biopolymers lost their function causing various diseases.

We create proteomimetic peptidic drug candidates that can replace the biological role of the non-functional proteins:

  • Step 1: we create a peptide with a distinct biological activity such as  enzyme inhibition, cell membrane penetration, antiviral or antifungal effect.

  • Step 2: this peptide is conjugated to a small molecule with a desired pharmacological effect, but different mode of action.


The proteomimetic conjugate possesses higher biological activity than those of its building blocks.

Development Phase


Novel Furin Inhibitor
to fight Covid-19 infections

Mechanism of Action of Emerging Treatments

COVID-19 Zoonosis and Cell Entry

Trends in Immunology 2020, 41, 271-273

The Furin

Furin is a cellular endoprotease that was identified in 1990; it proteolytically activates large numbers of proprotein substrates in secretory pathway compartments. Furin also has an essential role in embryogenesis, and catalyses the maturation of a strikingly diverse collection of proprotein substrates. These range from growth factors and receptors to extracellular-matrix proteins and even other protease systems that control disease.

Furin is an Entrance door  for

  • viruses: HIV, influenza, dengue fever, ebola marburg virus, COVID-19

  • bacterial toxins


Furin plays an important role in tumour genesis and development.


Issues limiting the clinical application of Furin inhibitors:

  • proteolytic instability

  • difficulty in synthesis

  • no possibilities for local application leading to systemic side effects (ubiquiter protein)

Physiological and pathological role of Furin

Clinical & Translational Immunology 2019; 8: e1073

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