Trilomer® peptidomimetics address a larger binding surface than small molecules, and are more robust than monoclonal antibodies.
Using N-methyl, N-alkyl and D-amino acids makes our fully synthetic Trilomer® molecules inherently resistant to proteases at the disease site, in the GI tract, or in the lysosome, greatly increases oral bioavailability and circulating half life.
Using unique synthesis conditions and a proprietary method of DNA encoding, our libraries contain millions of compounds in a single tube.
We are focused on the discovery of innovative treatments for the world's toughest diseases
Our Trilomer® platform of peptidomimetic binders allows for the targeted inhibition of disease-causing proteins, for the treatment of cancer, autoimmune diseases, infectious diseases, and others. In a revolution of therapeutic approaches, Trilomer® peptidomimetic binders combine the cell permeability and degradation resistance of small molecules with the large surface area of antibodies, allowing them to target both intracellular and extracellular targets. Due to their fully synthetic modular building blocks, affinity optimization and structure-activity relationships (SAR) can be performed much more rapidly than either traditional medicinal chemistry or targeted mutagenesis of biologics.
Our Degradomer® class of targeted protein degraders expands on the Trilomer® concept, allowing highly specific degradation of disease-causing proteins, including so-called “undruggable” targets like K-Ras, β-catenin, FoxP3, CBLB, and BIRC5/survivin.
Can target any disease-causing protein
DNA encoded library with millions of peptidomimetics
Protease resistant due to N-methyl, N-alkyl, and D-amino acids
Decades of research by scientists around the world have revealed which mutated proteins are the true drivers of the disease.
Only a small fraction of these contain an enzymatic pocket amenable to targeting with traditional pharmaceutics, or reside on the surface of the cell where they can be targeted with monoclonal antibodies.
The remaining mutated proteins are often called "undruggable". They are typically either protein-protein interacting (PPI) molecules, or protein-DNA interacting (transcription factors).
Examples include KRAS(G12D/G12V) – a key driver of pancreatic cancer, and β-catenin – a key driver of colorectal cancer.
well-validated driver of disease
model of mutant protein inhibition
Dr. Wilson was previously CSO at Oxford Biotherapeutics, and Director of Discovery at AbbVie. He has extensive experience of developing and executing new technology platforms, novel discovery programs, and clinical and portfolio strategies, resulting in over 30 pre-IND clinical development programs and more than 10 clinical trials. Currently he is a founder of two early phase technology and drug development companies.
Dr. Gish started his career in cancer research with scientist positions at Affymetrix and Eos Biotechnology, and later was Director of Biologics Technologies at PDL BioPharma and Research Fellow at AbbVie. With his expertise in target discovery and therapeutics development, Kurt has led products from concept into phase I human trials and is the inventor on 24 issued US patents.
Mr. Steinmiller has 20 years’ experience developing devices for biomedical research and diagnostics, resulting in 22 issued patents covering chemical synthesis, fluidics, and chemical analysis. He co-founded and raised venture financing for Claros Diagnostics which was acquired by OPKO Health, where he served as COO of OPKO Diagnostics.
Board of Directors
Staff Scientist, Chemical Biology
2019: Recipient of National Science Foundation grant for Small Business Innovation Research
2019: Recipient of Golden Ticket Award by AbbVie
2020: Recipient of Golden Ticket Award by Amgen
Listen to Trilo's CEO and Co-Founder, Dr. Kurt Gish, give an overview of
Trilo's approach for developing a new class of pharmaceutical drugs.
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