Policy & Regulation
Bicycle Therapeutics Adds to Clinical Team to Advance Pipeline
15 May 2019 - - UK-based biopharmaceutical company Bicycle Therapeutics has hired Lisa Mahnke, M.D., Ph.D. as senior vice president and head of clinical and Terrence West, MBA as vice president and head of program management, the company said.

Mahnke has completed multiple successful investigational new drug applications and brings deep expertise in pharmaceutical development to Bicycle, including experience in clinical development, clinical pharmacology and translational medicine.

West is a seasoned biopharma executive with experience across multiple therapeutic areas and project functions.

Lisa Mahnke will lead Bicycle's clinical efforts. Most recently, Dr. Mahnke was head of clinical development at Dragonfly Therapeutics and Syros Pharmaceuticals.

Before that, she held positions of increasing responsibility in clinical pharmacology and clinical development, including medical lead and head of clinical pharmacology, at BMS, Merck, EMD Serono and Vertex Pharmaceuticals.

She is a licensed and prior board-certified physician in internal medicine and infectious diseases. Dr. Mahnke holds a B.S. in chemistry from Ripon College, a Ph.D. in biochemistry and an M.D. from the University of Wisconsin-Madison.

Terrence West was most recently Executive director, Project Management, at EMD Serono, where he successfully led multiple teams from discovery through initial FDA filings, including Phase I-III clinical program approvals and launches.

He has also worked in program management for companies including ZioPharm Oncology, Stryker Regenerative Medicine, Dynavax Technologies and Exelixis, Inc. West holds a B.S. in chemistry from the University of Arizona and an MBA in Technology Management from the University of Phoenix.

Bicycle Therapeutics is a clinical-stage biopharmaceutical company developing a novel class of medicines, referred to as Bicycles, for diseases that are underserved by existing therapeutics. Bicycles are fully synthetic short peptides constrained to form two loops that stabilize their structural geometry.

This constraint is designed to confer high affinity and selectivity, and the relatively large surface area presented by the molecule allows targets to be drugged that have historically been intractable to non-biological approaches.
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