Ghrelin [1-27] peptide

Ghrelin [1-27] peptide

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

H-GSSFLSPEHQRVQQRKESKKPPAKLQP-OH

H-Gly-Ser-Ser-Phe-Leu-Ser-Pro-Glu-His-Gln-Arg-Val-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-OH

27

95.13%

C₁₃₅H₂₂₃N₄₃O₄₀

3088.46

Synthetic

Powder

Ghrelin [1-27] is a synthetic peptide derived from ghrelin, a 28-amino acid peptide that acts as an endogenous ligand for the growth hormone secretagogue receptor (GHS-R).
Ghrelin [1-27] lacks the C-terminal Arg 28 residue found in the full-length ghrelin peptide. It is one of the ghrelin-derived molecules that were isolated and characterized during the purification of human ghrelin from the stomach.
Synthetic Ghrelin [1-27] has been shown to induce increases in intracellular calcium levels in cells expressing GHS-R, similar to other ghrelin forms such as ghrelin, decanoyl ghrelin, and decanoyl ghrelin-(1-27).

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

• Hosoda H, Kojima M, Mizushima T, Shimizu S, Kangawa K. Structural divergence of human ghrelin. Identification of multiple ghrelin-derived molecules produced by post-translational processing. J Biol Chem. 2003;278(1):64-70.

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.