Buffalo Milk Casein Derived Decapeptide

Buffalo Milk Casein Derived Decapeptide

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

Batch to batch variation of the purity

H-YQEPVLGPVR-OH

H-Tyr-Gln-Glu-Pro-Val-Leu-Gly-Pro-Val-Arg-OH

10

95.23%

C₅₃H₈₄N₁₄O₁₅

1157.31

Synthetic

Powder

Buffalo casein derived decapeptide (YQEPVLGPVR) displayed anti-inflammatory response by suppressed (p<0.01) murine splenocytes proliferation, reduced inflammatory cytokine levels (Interferon-γ) besides elevated levels of regulatory cytokines (Interleukin-10 and Transforming Growth Factor-β) in splenocyte culture supernatant. Decapeptide also improved the phagocytosis (p<0.01) of peritoneal macrophages. This peptide was identified during enzymatic digestion of β-casein from Indian buffalo and cross bred cattle milk.

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

• Sowmya, K., Bhat, M.I., Bajaj, R.K. et al. Buffalo Milk Casein Derived Decapeptide (YQEPVLGPVR) Having Bifunctional Anti-inflammatory and Antioxidative Features Under Cellular Milieu. Int J Pept Res Ther 25, 623-633 (2019). https://doi.org/10.1007/s10989-018-9708-7

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.