RG33 peptide

RG33 peptide

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

Ac-PALEDLRQGLLPVLESFKVSFLSALEEYTKKLN-NH2

Ac-Pro-Ala-Leu-Glu-Asp-Leu-Arg-Gln-Gly-Leu-Leu-Pro-Val-Leu-Glu-Ser-Phe-Lys-Val-Ser-Phe-Leu-Ser-Ala-Leu-Glu-Glu-Tyr-Thr-Lys-Lys-Leu-Asn-NH2

33

95.29%

C₁₇₅H₂₈₂N₄₂O₅₁

3790.34

Synthetic

Powder

RG33 is a peptide corresponding to the two last helical segments, amino acid residues 209–241 of apolipoprotein A1 (ApoA-I), the major protein component of high-density lipoprotein (HDL) particles in plasma. ApoA-I has a specific role in lipid metabolism and enables efflux of molecules by accepting fats from within cells for transport and metabolism elsewhere. In vivo RG33 peptide efficiently solubilizes lipid vesicles, and promotes the efflux of cholesterol from cultured macrophages. In vitro RG33 peptide significantly improves the glucose clearance capacity of insulin resistant mice and provides systemic glucose control in an insulin resistant mouse model.

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

• Edmunds et al (2020) A short peptide of the C-terminal class Y helices of apolipoprotein A-I has preserved functions in cholesterol efflux and in vivo metabolic control. Sci. Rep. 10 18070 PMID: 33093642

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.