James T. Daniel

TL;DR: Structural determination by NMR spectroscopy helped to identify a simplified biologically active eight residue peptide motif containing a single disulfide bond that is an excellent lead molecule for developing a new generation of analgesic peptide drugs.

TL;DR: Findings suggest that selectively targeting GABABR-mediated HVA calcium channel inhibition by α-conotoxins could be effective for the treatment of chronic visceral pain.

TL;DR: The current state of knowledge regarding venom peptides that target GPCRs to produce analgesia, and their development as therapeutic compounds are reviewed.

TL;DR: The molecular engineering approaches that have been used to modify these conotoxins to improve their pharmacological properties, including potency, selectivity, stability, and minimisation of the bioactive pharmacophore are discussed.

TL;DR: Investigation of whether alternative helical inducing strategies also can enhance structure and activity at RXFP3 found neither dicarba variants nor Thr21 as a putative new receptor contact residue important for RX FP3 binding found.