We are changing the status quo to make the impossible possible, by expanding the scope of new targets for drug development through targeted protein manipulation.

Chaperone-mediated Autophagy Protein Degradation Technology (CHAPTAC)

Targeted protein degradation has the potential to unlock a large number of targets that are considered "undruggable," by traditional drug discovery methods. This presents a significant opportunity for developing new therapeutics by destroying the disease-causing proteins through specific techniques.

We have developed a proprietary protein degradation platform that overcomes the current limitations of existing protein degradation techniques. Our proprietary CHAPTAC technology is unique as it reversibly degrades the disease proteins either via the lysosome or the proteasome degradation machineries of the cell. We have demonstrated that our CHAPTAC technology is more versatile than PROTAC technology in cases where the proteasome is dysfunctional. Since our peptides are made of natural amino acids, they are degraded together with the target protein, and consequently have less toxicity compared with thalidomide-based PROTAC methods of targeted protein degradation. By removing pathogenic proteins from the body, we believe this will lead to more extensive and sustained therapeutic benefits.

Below is a simple, non-virally mediated, cell membrane—permeant, targeting peptide—based system that rapidly and reversibly degrades an endogenous protein of interest through lysosomal degradation.

How we eliminate disease causing target proteins via the lysosome

lysosomal degradation

The steps in our technology are as follows:

  1. We identify the specific protein binding sequence of a target of interest.
  2. We construct the targeting peptide which consists of three parts:
    1. cell-penetrating domain that delivers the specific peptide across the blood-brain barrier and the plasma membrane of cells;
    2. a short target protein-binding domain that specifically binds to the target protein of interest with high affinity; and
    3. the chaperone-mediated autophagy (CMA)-targeting motif (CTM) that directs the peptide-protein complex for lysosomal degradation.
  3. The targeting peptide drug binds to the disease-causing protein.
  4. The targeting peptide traffics the disease-causing protein to the lysosome.
  5. The lysosome efficiently degrades both.


Our proprietary CHAPTAC technology offers several key advantages over leading competitive protein degradation techniques, in particular, PROTAC, Antisense Oligonucleotides and siRNA, as well as CRISPR/Cas9.


Characteristics CHAPTAC PROTAC Antisense Oligonucleotide and siRNA CRISPR/Cas9
Low toxicity X X X
Ease of manufacturing MAYBE X
Ease of finding a new molecule X
Blood-brain barrier and cell permeability MAYBE X X
Can target post-translationally modified proteins X X
Rapid protein degradation onset X X
Degrades "undruggable" targets
Reversible protein knockdown X

We have validated our CHAPTAC technology in vitro and in vivo with multiple protein targets in cardiovascular, neurological and cancer indications.



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