Neuromedin C peptide

Neuromedin C peptide

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

Batch to batch variation of the purity

H-GNHWAVGHLM-NH2

H-Gly-Asn-His-Trp-Ala-Val-Gly-His-Leu-Met-NH2

10

95.9%

C₅₀H₇₃N₁₇O₁₁S

1120.28

Synthetic

Powder

Neuromedin C is a decapeptide identified in porcine spinal cord. It was purified from a side fraction obtained during the isolation of neuromedin B. The amino acid sequence of Neuromedin C is Gly-Asn-His-Trp-Ala-Val-Gly-His-Leu-Met-NH₂. It is identical to the carboxy-terminal subsequence [18-27] of gastrin releasing peptide (GRP). Neuromedin C exhibits a potent contractile activity on rat uterus in a characteristic manner similar to bombesin. It is thought to be a neuromediator in the neural communication systems of mammals. The peptide was named "neuromedin C" due to its close relationship with "neuromedin B", another bombesin-like mammalian peptide. Compared to other bombesin-like peptides, Neuromedin C has about 60% of the potency of bombesin and is more potent than GRP. Its decapeptide structure is considered the minimum molecule capable of eliciting the full spectrum of bombesin-like activity, and it is likely processed from GRP or its precursor in neural tissues.

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

• Minamino N, Kangawa K, Matsuo H. Neuromedin C: a bombesin-like peptide identified in porcine spinal cord. Biochem Biophys Res Commun. 1984 Feb 29;119(1):14-20. doi: 10.1016/0006-291x(84)91611-5. PMID: 6546686.

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.