TY - JOUR
T1 - Identification, Synthesis, Conformation and Activity of an Insulin-like Peptide from a Sea Anemone
AU - Mitchell, Michela L.
AU - Hossain, Mohammed Akhter
AU - Lin, Feng
AU - Pinheiro‐junior, Ernesto L.
AU - Peigneur, Steve
AU - Wai, Dorothy C.C.
AU - Delaine, Carlie
AU - Blyth, Andrew J.
AU - Forbes, Briony E.
AU - Tytgat, Jan
AU - Wade, John D.
AU - Norton, Raymond S.
PY - 2021/12
Y1 - 2021/12
N2 - The role of insulin and insulin‐like peptides (ILPs) in vertebrate animals is well studied. Numerous ILPs are also found in invertebrates, although there is uncertainty as to the function and role of many of these peptides. We have identified transcripts with similarity to the insulin family in the tentacle transcriptomes of the sea anemone Oulactis sp. (Actiniaria: Actiniidae). The translated transcripts showed that these insulin‐like peptides have highly conserved A‐ and B‐chains among individuals of this species, as well as other Anthozoa. An Oulactis sp. ILP sequence (IlO1_i1) was synthesized using Fmoc solid‐phase peptide synthesis of the individual chains, followed by regi-oselective disulfide bond formation of the intra‐A and two interchain disulfide bonds. Bioactivity studies of IlO1_i1 were conducted on human insulin and insulin‐like growth factor receptors, and on voltage‐gated potassium, sodium, and calcium channels. IlO1_i1 did not bind to the insulin or insulin‐like growth factor receptors, but showed weak activity against KV1.2, 1.3, 3.1, and 11.1 (hERG) channels, as well as NaV1.4 channels. Further functional studies are required to determine the role of this peptide in the sea anemone.
AB - The role of insulin and insulin‐like peptides (ILPs) in vertebrate animals is well studied. Numerous ILPs are also found in invertebrates, although there is uncertainty as to the function and role of many of these peptides. We have identified transcripts with similarity to the insulin family in the tentacle transcriptomes of the sea anemone Oulactis sp. (Actiniaria: Actiniidae). The translated transcripts showed that these insulin‐like peptides have highly conserved A‐ and B‐chains among individuals of this species, as well as other Anthozoa. An Oulactis sp. ILP sequence (IlO1_i1) was synthesized using Fmoc solid‐phase peptide synthesis of the individual chains, followed by regi-oselective disulfide bond formation of the intra‐A and two interchain disulfide bonds. Bioactivity studies of IlO1_i1 were conducted on human insulin and insulin‐like growth factor receptors, and on voltage‐gated potassium, sodium, and calcium channels. IlO1_i1 did not bind to the insulin or insulin‐like growth factor receptors, but showed weak activity against KV1.2, 1.3, 3.1, and 11.1 (hERG) channels, as well as NaV1.4 channels. Further functional studies are required to determine the role of this peptide in the sea anemone.
KW - Cnidaria
KW - Insulin
KW - Invertebrates
KW - Ion channel
KW - Oulactis
KW - Peptide synthesis
UR - http://www.scopus.com/inward/record.url?scp=85120085569&partnerID=8YFLogxK
UR - http://purl.org/au-research/grants/ARC/LP150100621
U2 - 10.3390/biom11121785
DO - 10.3390/biom11121785
M3 - Article
AN - SCOPUS:85120085569
VL - 11
JO - Biomolecules
JF - Biomolecules
SN - 2218-273X
IS - 12
M1 - 1785
ER -