LEXINGTON, Mass. — TRIANA Biomedicines, Inc. announced that the first patient has been dosed in a Phase 1/2 clinical trial evaluating TRI-611, an investigational therapy for patients with anaplastic lymphoma kinase–positive (ALK+) non-small cell lung cancer (NSCLC).
TRI-611 is an oral small molecule designed as a brain-penetrant molecular glue degrader that targets ALK fusion proteins for destruction by engaging the body’s natural protein-degradation system. The trial initiation marks a key milestone for the company’s molecular glue degrader platform.
“Dosing of the first patient with TRI-611 marks an important milestone for TRIANA and for the ALK+ NSCLC patient community,” said Dr. Patrick Trojer, CEO & President of TRIANA. “This study reflects our commitment to treating diseases in entirely new ways.”
Non-small cell lung cancer accounts for about 85 percent of all lung cancer cases, with ALK+ NSCLC representing a subset driven by ALK fusion proteins. While targeted therapies such as ALK tyrosine kinase inhibitors have improved outcomes, many patients eventually develop resistance, and treatment options remain limited, particularly for younger, non-smoking populations.
The ongoing Phase 1/2 study is a global, first-in-human, open-label trial designed to evaluate the safety, tolerability, pharmacokinetics, and preliminary anti-tumor activity of TRI-611. The Phase 1 portion includes dose escalation in patients previously treated with standard-of-care ALK inhibitors, while Phase 2 will further assess safety and efficacy across multiple patient groups.
“We are excited to have TRI-611 in the clinic and to advance this new potential therapy for people living with lung cancer,” said Dr. Caroline Germa, Chief Medical Officer of TRIANA. “Despite progress in treatments, many patients continue to face limited options. This study represents an important step in our mission to develop innovative therapies that may ultimately improve outcomes for ALK+ NSCLC patients and their families.”
TRI-611 is designed to selectively degrade ALK fusion proteins by bringing them into proximity with the E3 ligase cereblon through a mechanism independent of the kinase active site. The approach aims to overcome limitations associated with currently available ALK inhibitors.
