ArticlePeptides2008
Conorfamide-Sr2, a gamma-carboxyglutamate-containing FMRFamide-related peptide from the venom of Conus spurius with activity in mice and mollusks.
Article in Peptides, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 35 citations in OpenAlex.
- Toxins in disguise: Neuropeptide mimicry across animal venoms.General and comparative endocrinology · 2026Review
- Identification of Novel Conotoxin Precursors from the Cone SnailMarine drugs · 2021Article
- A phylogeny-aware approach reveals unexpected venom components in divergent lineages of cone snails.Proceedings. Biological sciences · 2021Article
- Hormone-like conopeptides - new tools for pharmaceutical design.RSC medicinal chemistry · 2020Review
- Neuropeptide signalling systems - An underexplored target for venom drug discovery.Biochemical pharmacology · 2020Review
- Studies of Conorfamide-Sr3 on Human Voltage-Gated Kv1 Potassium Channel Subtypes.Marine drugs · 2020Article
- Structural and Functional Characterization of Conotoxins fromMarine drugs · 2020Article
- Marine Natural Products from the Yucatan Peninsula.Marine drugs · 2020Review
- Conopeptides promote itch through human itch receptor hMgprX1.Toxicon : official journal of the International Society on Toxinology · 2018Article
- Identification of a cono-RFamide from the venom ofProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Regulating Factors in Acid-Sensing Ion Channel 1a Function.Neurochemical research · 2016Review
- In the picture: disulfide-poor conopeptides, a class of pharmacologically interesting compounds.The journal of venomous animals and toxins including tropical diseases · 2016Review
- Discovery by proteogenomics and characterization of an RF-amide neuropeptide from cone snail venom.Journal of proteomics · 2015Article
- Diversity of the RFamide Peptide Family in Mollusks.Frontiers in endocrinology · 2014Review
- Functional hypervariability and gene diversity of cardioactive neuropeptides.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
A novel peptide, conorfamide-Sr2 (CNF-Sr2), was purified from the venom extract of Conus spurius, collected in the Caribbean Sea off the Yucatan Peninsula. Its primary structure was determined by automated Edman degradation and amino acid analysis, and confirmed by electrospray ionization mass spectrometry. Conorfamide-Sr2 contains 12 amino acids and no Cys residues, and it is only the second FMRFamide-related peptide isolated from a venom. Its primary structure GPM gammaDPLgammaIIRI-nh2, (gamma, gamma-carboxyglutamate; -nh2, amidated C-terminus; calculated monoisotopic mass, 1468.72Da; experimental monoisotopic mass, 1468.70Da) shows two features that are unusual among FMRFamide-related peptides (FaRPs, also known as RFamide peptides), namely the novel presence of gamma-carboxyglutamate, and a rather uncommon C-terminal residue, Ile. CNF-Sr2 exhibits paralytic activity in the limpet Patella opea and causes hyperactivity in the freshwater snail Pomacea paludosa and in the mouse. The sequence similarities of CNF-Sr2 with FaRPs from marine and freshwater mollusks and mice might explain its biological effects in these organisms. It also resembles FaRPs from polychaetes (the prey of C. spurius), which suggests a natural biological role. Based on these similarities, CNF-Sr2 might interact with receptors of these three distinct types of FaRPs, G-protein-coupled receptors, Na+ channels activated by FMRFamide (FaNaCs), and acid-sensing ion channels (ASICs). The biological activities of CNF-Sr2 in mollusks and mice make it a potential tool to study molecular targets in these and other organisms.
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