Amphista Therapeutics closes £6m funding round



Amphista Therapeutics, a University of Dundee spin-out, has announced a multi-million-pound deal to develop first-in-class cancer therapeutics that harness the body’s natural processes to selectively and efficiently degrade and remove disease-causing proteins.

Professor Alessio Ciulli

The spin-out has announced the closing of a £6 million Series A round, led by Advent Life Sciences. Seed round funders the Scottish Investment Bank, with backing from the Scottish Growth Scheme, and the European Investment Fund joined the round, along with new investor, US-based life sciences BioMotiv.

Amphista’s scientific founder, Professor Alessio Ciulli, based at the University of Dundee, is an internationally renowned expert in the field of targeted protein degradation (TPD). He said: “Highly specific TPD is a transformative new modality for tackling previously undruggable targets with high therapeutic value.” 

 Nicola Thompson, Amphista’s CEO, said: “This international financing provides Amphista with a firm foundation to underpin a Series B round to progress our oncology pipeline to the clinic. Our vision is to create a leading protein degradation company on the global stage that delivers ground-breaking new medicines to patients in areas of high unmet need.”

Raj Parekh, general partner at lead investor, Advent Life Sciences, added: “We are excited to support Amphista in its next stage of development. The Company has a potentially unique approach to targeted protein degradation when compared with traditional proteolysis targeting chimera (PROTAC®) platforms. We believe that Amphista has great potential with its differentiated proprietary technology to address traditionally undruggable targets.”

Amphista’s TPD small molecules instruct the cell to degrade the target directly rather than activating or inhibiting the target protein function. As protein-protein interactions are involved in disease progression, removing the target protein provides a clear therapeutic advantage over simple inhibition.

 



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