TY - JOUR
T1 - Strategies for the development of conotoxins as new therapeutic leads
AU - Brady, Ryan
AU - Baell, Jonathan Bayldon
AU - Norton, Raymond Stanley
PY - 2013
Y1 - 2013
N2 - Peptide toxins typically bind to their target ion channels or receptors with high potency and selectivity, making them attractive leads for therapeutic development. In some cases the native peptide as it is found in the venom from which it originates can be used directly, but in many instances it is desirable to truncate and/or stabilize the peptide to improve its therapeutic properties. A complementary strategy is to display the key residues that make up the pharmacophore of the peptide toxin on a non-peptidic scaffold, thereby creating a peptidomimetic. This review exemplifies these approaches with peptide toxins from marine organisms, with a particular focus on conotoxins.
AB - Peptide toxins typically bind to their target ion channels or receptors with high potency and selectivity, making them attractive leads for therapeutic development. In some cases the native peptide as it is found in the venom from which it originates can be used directly, but in many instances it is desirable to truncate and/or stabilize the peptide to improve its therapeutic properties. A complementary strategy is to display the key residues that make up the pharmacophore of the peptide toxin on a non-peptidic scaffold, thereby creating a peptidomimetic. This review exemplifies these approaches with peptide toxins from marine organisms, with a particular focus on conotoxins.
UR - http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3736424/pdf/marinedrugs-11-02293.pdf
U2 - 10.3390/md11072293
DO - 10.3390/md11072293
M3 - Article
VL - 11
SP - 2293
EP - 2313
JO - Marine Drugs
JF - Marine Drugs
SN - 1660-3397
IS - 7
ER -