Conorfamide-Sr2 peptide

Conorfamide-Sr2 peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

H-GPMEDPLEIIRI-NH2

H-Gly-Pro-Met-Glu-Asp-Pro-Leu-Glu-Ile-Ile-Arg-Ile-NH2

12

95.61%

C₆₁H₁₀₄N₁₆O₁₈S

1381.63

Synthetic

Powder

Conorfamide-Sr2 (CNF-Sr2), was purified from the venom extract of alphabet cone (Conus spurius), collected in the Caribbean Sea off the Yucatan Peninsula.
Conorfamide-Sr2 is the second FMRFamide-related peptide isolated from the venom, and the glutamic acids in this sequence are gamma-carboxyglutamate acids.
Conorfamide-Sr2 exhibits paralytic activity in the limpet Patella opea and causes hyperactivity in the freshwater snail Pomacea paludosa and the mouse. The sequence similarities of Conorfamide-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, Conorfamide-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 Conorfamide-Sr2 in mollusks and mice make it a potential tool to study molecular targets in these and other organisms.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides

• Aguilar MB, Luna-ramírez KS, Echeverría D, et al. Conorfamide-Sr2, a gamma-carboxyglutamate-containing FMRFamide-related peptide from the venom of Conus spurius with activity in mice and mollusks. Peptides. 2008;29(2):186-95.
• Campos-Lira E, Carrillo E, Aguilar MB, Gajewiak J, Gómez-Lagunas F, López-Vera E. Conorfamide-Sr3, a structurally novel specific inhibitor of the Shaker K+ channel. Toxicon. 2017 Nov;138:53-58.
• Espino SS, Robinson SD, Safavi-Hemami H, Gajewiak J, Yang W, Olivera BM, Liu Q. Conopeptides promote itch through human itch receptor hMgprX1. Toxicon. 2018 Nov;154:28-34.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.