TY - CONF
T1 - Correlations among sequence, physicochemical properties and function in peptide toxins
AU - Norton, Raymond S.
AU - Mitchell, Michela L.
AU - Shafee, Thomas
PY - 2020/4/20
Y1 - 2020/4/20
N2 - Sea anemones are a rich source of peptides that are potent and often selective probes of the structure and function of ion channels and receptors. For example, several peptides from sea anemones and analogues thereof are potent blockers of the voltage-gated potassium channel Kv1.3, which plays a major role in the activation of effector memory T cells. As these cells have a key role in autoimmune diseases such as multiple sclerosis, psoriasis, type 1 diabetes and rheumatoid arthritis, peptide blockers of Kv1.3that selectively inhibit the activation of TEM cells show considerable potential as therapeutics for autoimmune diseases. These and other studies of sea anemones highlight how widespread the ShK fold is in nature, not only in the phylum Cnidaria, but also in parasitic worms mammals and even plants. A comparison of available ShK sequences based on various physicochemical properties reveals that they cluster into discrete sub-sets; the relationships among these clusters, their functional activity and potential as therapeutics are currently being explored, but it is clear that this fold can support several other activities beyond potassium channel blockade.
AB - Sea anemones are a rich source of peptides that are potent and often selective probes of the structure and function of ion channels and receptors. For example, several peptides from sea anemones and analogues thereof are potent blockers of the voltage-gated potassium channel Kv1.3, which plays a major role in the activation of effector memory T cells. As these cells have a key role in autoimmune diseases such as multiple sclerosis, psoriasis, type 1 diabetes and rheumatoid arthritis, peptide blockers of Kv1.3that selectively inhibit the activation of TEM cells show considerable potential as therapeutics for autoimmune diseases. These and other studies of sea anemones highlight how widespread the ShK fold is in nature, not only in the phylum Cnidaria, but also in parasitic worms mammals and even plants. A comparison of available ShK sequences based on various physicochemical properties reveals that they cluster into discrete sub-sets; the relationships among these clusters, their functional activity and potential as therapeutics are currently being explored, but it is clear that this fold can support several other activities beyond potassium channel blockade.
UR - http://www.scopus.com/inward/record.url?scp=85087718632&partnerID=8YFLogxK
U2 - 10.1016/j.toxicon.2019.10.074
DO - 10.1016/j.toxicon.2019.10.074
M3 - Abstract
C2 - 32634934
AN - SCOPUS:85087718632
SP - S17-S17
ER -
