Scientists from UNIGE have developed synthetic molecules that mimic antibodies. They could revolutionize the treatment of certain diseases.
Synthetic antibodies have become the cornerstone of cancer therapies. This approach was also favored in the initial fight against COVID-19. However, their laboratory production is time-consuming and costly.
The two parts of the SAP molecule are shown in blue and red. They are connected by strands of peptide nucleic acid (PNA).
© Winssinger - UNIGE
A team from the University of Geneva (UNIGE) has developed a new technology called
Self-Assembled Proteomimetics (SAPs). It offers a faster and more affordable way to create synthetic molecules that act like antibodies. This new approach could revolutionize treatments for diseases such as cancer and COVID-19. These findings are published in the
Proceedings of the National Academy of Sciences (PNAS).
Monoclonal antibodies are essential for biomedical research and cancer treatments due to their targeted action. These laboratory-made molecules act like the natural antibodies in our immune system, each designed to bind to a specific protein. This precision allows them to effectively target certain cells, such as tumor cells or viruses. However, despite their effectiveness, monoclonal antibodies are complex to design, which limits their application.
SAPs are easier and less expensive to produce
A group from the Section of Chemistry and Biochemistry at UNIGE, led by Nicolas Winssinger, full professor in the Department of Organic Chemistry at the Faculty of Science of UNIGE, is opening a new paradigm for the design of drugs targeting proteins, capable of replacing monoclonal antibodies: self-assembled proteomimetics (SAPs).
SAPs are tiny molecules custom-designed to target and neutralize harmful proteins in the body, much like antibodies. The difference? "SAPs are easier and less expensive to produce. They are designed as a two-part system. Like puzzle pieces, these components fit together to form a stable structure capable of tightly binding to pathogenic proteins. This innovative design mimics the precise and powerful function of antibodies, while eliminating many of the challenges associated with their production," explains Nicolas Winssinger.
More specifically, SAPs consist of two "pieces," each about 30 amino acids long, tightly linked by strands of peptide nucleic acid (PNA), a synthetic polymer whose structure is similar to DNA and RNA. These miniproteins can be easily produced in the laboratory. The effectiveness of this new approach is demonstrated on important therapeutic targets, namely HER2, a well-known cancer biomarker, or by targeting the SARS-CoV-2 Spike protein receptor.
Furthermore, the researchers have shown that PNA can be dynamically controlled to adjust the degree of binding of SAPs to their targets. This capability could prove very useful in therapeutic applications, allowing precise control of therapeutic activity.
By making these synthetic molecules accessible and effective, SAPs have the potential to transform how we treat complex diseases and make this type of therapy more accessible.