Bombesin peptide

Bombesin peptide

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

Batch to batch variation of the purity

Pyr-QRLGNQWAVGHLM

pGlu-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2

14

97.7%

C₇₁H₁₁₀N₂₄O₁₈S

1619.8

Synthetic

Powder

Bombesin is a peptide that was originally isolated from the skin of the European frog Bombina bombina. It is a tetradecapeptide with a COOH terminus ending in Gly-His-Leu-Met NH₂. Bombesin is closely related to two mammalian peptides, gastrin-releasing peptide (GRP) and neuromedin B (NMB).
GRP is a 27-amino acid peptide originally isolated from porcine stomach, which shares the same seven COOH terminal amino acids with Bombesin. The human GRP-encoding gene is on chromosome 18q21, and GRP is widely distributed in the central nervous system and peripheral tissues, especially in the gastrointestinal (GI) tract.
NMB is a decapeptide isolated from porcine spinal cord, which is similar to the frog peptide ranatensin. The human NMB gene is on chromosome 15q11. NMB is also distributed in the GI tract and the central nervous system.
The actions of these peptides are mediated by three closely related receptors: the GRP-preferring receptor (BB₂-receptor), the NMB-preferring receptor (BB₁-receptor), and the orphan receptor bombesin-receptor-subtype-3 (BB₃-receptor). These receptors are G protein-coupled receptors that signal primarily through phospholipase C-mediated cascades.

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

• Anastasi A, Erspamer V, Bucci M. Isolation and amino acid sequences of alytesin and bombesin, two analogous active tetradecapeptides from the skin of European discoglossid frogs. Arch Biochem Biophys. 1972;148(2):443-6.
• Gonzalez N, Moody TW, Igarashi H, Ito T, Jensen RT. Bombesin-related peptides and their receptors: recent advances in their role in physiology and disease states. Curr Opin Endocrinol Diabetes Obes. 2008 Feb;15(1):58-64. doi: 10.1097/MED.0b013e3282f3709b. PMID: 18185064; PMCID: PMC2631407.

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.