N-Terminal (Edman) sequencing

More effective analgesics with fewer side-effects are required to treat chronic pain. In conjunction with Professor Glenn King and colleagues at the University of Queensland’s Institute for Molecular Bioscience, APAF has been a longer-term partner in determining venom peptide primary structures through Edman sequencing. Recently, the team reported the discovery of Tp1a, a novel NaV1.7 inhibitor from the venom of a Peruvian tarantula.  APAF characterised the peptide by sequencing the first 31 amino acids of Tp1a. Tp1a is of interest as it inhibits sodium channels without significantly altering the voltage dependence of activation or inactivation. Furthermore, Tp1a proved to be analgesic by reversing spontaneous pain induced in mouse model.

Seven novel modulators of the analgesic target NaV1.7 uncovered using a high-throughput venom-based discovery approach
British Journal of Pharmacology DOI:10.1111/bph.13081 www.brjpharmacol.org