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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Identification, Synthesis, Conformation and Activity of an Insulin-like Peptide from a Sea Anemone

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Author(s):
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Mitchell, Michela L. [1, 2, 3] ; Hossain, Mohammed Akhter [4, 5] ; Lin, Feng [4] ; Pinheiro-Junior, Ernesto L. [6] ; Peigneur, Steve [6] ; Wai, Dorothy C. C. [1] ; Delaine, Carlie [7] ; Blyth, Andrew J. [7] ; Forbes, Briony E. [7] ; Tytgat, Jan [6] ; Wade, John D. [4, 5] ; Norton, Raymond S. [1, 8]
Total Authors: 12
Affiliation:
[1] Monash Univ, Med Chem, Monash Inst Pharmaceut Sci, 381 Royal Parade, Parkville, Vic 3052 - Australia
[2] Museum Victoria, Dept Sci, GPO Box 666, Melbourne, Vic 3001 - Australia
[3] Queensland Museum, Biodivers & Geosci, POB 3000, South Brisbane, Qld 4101 - Australia
[4] Univ Melbourne, Florey Inst Neurosci & Mental Hlth, Parkville, Vic 3010 - Australia
[5] Univ Melbourne, Sch Chem, Parkville, Vic 3010 - Australia
[6] Univ Leuven, Toxicol & Pharmacol, O&N 2, Herestr 49, POB 922, B-3000 Leuven - Belgium
[7] Flinders Univ S Australia, Flinders Hlth & Med Res Inst, Bedford Pk, SA 5042 - Australia
[8] Monash Univ, ARC Ctr Fragment Based Design, Parkville, Vic 3052 - Australia
Total Affiliations: 8
Document type: Journal article
Source: BIOMOLECULES; v. 11, n. 12 DEC 2021.
Web of Science Citations: 0
Abstract

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 regioselective 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 K(V)1.2, 1.3, 3.1, and 11.1 (hERG) channels, as well as Na(V)1.4 channels. Further functional studies are required to determine the role of this peptide in the sea anemone. (AU)

FAPESP's process: 16/04761-4 - Functional and structural characterization and immune response evaluation of a recombinant serine protease from Crotalus durissus collilineatus modified by PEGylation
Grantee:Ernesto Lopes Pinheiro Junior
Support Opportunities: Scholarships in Brazil - Doctorate (Direct)