beta-Conglycinin fragment P3 peptide

beta-Conglycinin fragment P3 peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

LLPHH

Leu-Leu-Pro-His-His

5

95.5%

C₂₉H₄₅N₉O₆

615.72

Synthetic

Powder

beta-Conglycinin fragment P3 was found in soybean (Glycine max). Bioactive peptides are prepared from both plant and animal sources, with the antihypertensive peptides IAP and VY and the hypocholesterolemic peptide IIAEK derived from wheat gliadin, sardine muscle, and bovine milk α-lactoglobulin, respectively. For soy protein, several bioactive peptides, including the hypocholesterolemic peptide LPYPR, antihypertensive peptide NWGPLV, antioxidant peptide LLPHH, and anti-obese peptide VRIRLLQRFNKRS, were derived from its major constituents, glycinin, and β-conglycinin (BCG).

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

• Inoue, N., Nagao, K., Sakata, K. et al. Screening of soy protein-derived hypotriglyceridemic di-peptides in vitro and in vivo. Lipids Health Dis 10, 85 (2011). https://doi.org/10.1186/1476-511X-10-85

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.