Bay 55-9837 peptide

Bay 55-9837 peptide

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

Batch to batch variation of the purity

H-HSDAVFTDNYTRLRKQVAAKKYLQSIKNKRY-NH2

H-His-Ser-Asp-Ala-Val-Phe-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-Gln-Val-Ala-Ala-Lys-Lys-Tyr-Leu-Gln-Ser-Ile-Lys-Asn-Lys-Arg-Tyr-NH2

31

95.77%

C₁₆₇H₂₇₀N₅₂O₄₆

3742.23

Synthetic

Powder

Bay 55-9837 is a selective vasoactive intestinal peptide receptor 2 (VPAC2 receptor) agonist, binding to VPAC2 with a Kd of 0.65 nmol/l and having greater than 100-fold selectivity over VPAC1. BAY 55-9837 stimulates glucose-dependent insulin secretion in isolated pancreatic islets, increases insulin synthesis in rat islets, and causes a dose-dependent increase in plasma insulin levels in fasted rats. BAY 55-9837 raises survival motor neuron (SMN) protein levels through pharmacological modulation of the SMN2 gene and ameliorates disease phenotype in severe spinal muscular atrophy mouse models

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

• Tsutsumi et al (2002) A potent and highly selective VPAC2 agonist enhances glucose-induced Ins release and glucose disposal: a potential therapy for type 2 diabetes. Diabetes 51 1453 PMID: 11978642
• Darsalia et al (2013)The specific VPAC2 agonist Bay 55-9837 increases neuronal damage and hemorrhagic transformation after stroke in type 2 diabetic rats. Neuropeptides 47(2) 133 PMID: 22981158
• Hadwen et al (2014) VPAC2 receptor agonist BAY 55-9837 increases SMN protein levels and moderates disease phenotype in severe spinal muscular atrophy mouse models. Orphanet J Rare Dis. 9 4 PMID: 24405637

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.