Sethera Therapeutics develops stable peptide therapeutics using a proprietary enzymatic cross-linking platform. This technology creates polymacrocyclic peptides (pMCPs) with enhanced stability and precise architecture for targeting challenging biological systems.
Funding
Funding not disclosed
Founders
Product
Problem
Developing peptide therapeutics that exhibit sufficient stability and target engagement for challenging biological systems remains a significant hurdle in drug discovery. Traditional peptide synthesis methods often struggle to produce complex, macrocyclic structures with the required stability and precise architecture for effective therapeutic intervention.
Solution
Sethera Therapeutics offers a proprietary platform for the synthesis of stable peptide therapeutics utilizing enzymatic cross-linking technology. This platform enables the creation of polymacrocyclic peptides (pMCPs) with unique architectures and chemistries, designed to interact with complex biological surfaces and modulate intricate pathways. The technology facilitates accelerated hit identification through streamlined enzymatic library creation and allows for precise tuning of peptide properties, including proteolytic stability and binding affinity, by incorporating noncanonical amino acids and modular recombination. This approach expands the accessible sequence-structure space, increasing the probability of identifying potent and stable peptide drug candidates for previously intractable targets.
Target Audience
Sethera Therapeutics targets pharmaceutical and biotechnology companies engaged in drug discovery and development, particularly those seeking novel therapeutic modalities for challenging biological targets.
Features
- Enzymatic cross-linking technology for site-specific thioether bond installation, enabling multiple macrocycle formations within a single peptide.
- Polymacrocyclic peptide (pMCP) Discovery Platform capable of constructing macrocycles ranging from 7 to 13 amino acids with up to 6 macrocycles per peptide.
- Support for combinatorial exploration of sequence and structure space, with the capacity to construct up to 20 unique architectural libraries in parallel.
- Compatibility with established screening techniques such as phage display, mRNA display, and DNA-encoded libraries.
- Ability to incorporate noncanonical amino acids and non-peptidic building blocks, allowing for extensive customization of peptide macrocycles.
- Modular recombination of pMCPs to create multi-valent binding motifs and imbue properties like membrane permeability and enhanced proteolytic stability.
- Platform agnostic to intervening residues beyond those directing cyclization, facilitating precise tuning of peptide properties.