SPARCs™ (Stabilized Peptides Against Receptors on Cancer) consist of a protein binding domain and may be functionalized with chemistry relevant to the linkers used in today’s radioligand therapy (RLT) products. Most current RLT products in development use small or large molecules to target cancer cell surface proteins, but those types of molecules are not ideal due to half-life, tissue penetration and amenability to different chemistries. Unlike these conventional targeting moieties and other peptide approaches, SPARCs are engineered to have several important properties:
Enhanced stability: constructed to be resistant to proteases, providing SPARCs advantages over other peptide approaches
Not immunogenic: given the clinical experience with our SPEARs™ and the same method for structural stability, we anticipate our SPARCs to be avoid off target immune activation
Proper half-life: the half-life of SPARCs is measured in days, compared to minutes/hours for small molecules and weeks/months for large molecules, enabling more precise clinical regimens
Tissue permeability: SPARCs are designed NOT to enter cells but rather track to their surface. Peptides will enable tissue penetration deeper than large molecules, providing greater access to the inside of tumor masses
Amenable to chemistry: As they are manufactured synthetically, SPARCs offer flexibility of chemical reactivity, from what type of functionality to where on the molecule it exists, well beyond the options provided by small and large molecules
A Robust Discovery Engine
We discover SPARCs through our Assay for Peptide Antagonist Discovery System (PADS™), which is built on our team’s years of experience in peptide chemistry and molecular and cancer biology.