VMPL peptide

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

Batch to batch variation of the purity

• VMPL polypeptide is a remarkable bioactive substance with significant potential in the field of health and medicine. It is derived from a natural source, specifically from the hydrolysis of tilapia viscera by-products. This polypeptide exhibits a molecular weight of 458.62g/mol and is composed of a unique sequence of amino acids.
• VMPL polypeptide has been demonstrated to possess notable biological activities. It shows inhibitory effects on the dipeptidyl peptidase IV (DPP-IV) enzyme, which plays a crucial role in glucose metabolism. By interacting with the DPP-IV enzyme, VMPL polypeptide helps maintain the activity of glucagon-like peptide-1 (GLP-1), thereby contributing to the regulation of blood sugar levels. This property makes it a promising candidate for the management of type-2 diabetes mellitus and other metabolic disorders.
• Furthermore, VMPL polypeptide is predicted to have excellent pharmacokinetic properties. It is non-toxic and has good cell penetrability, ensuring its safety and effectiveness in vivo. Additionally, it demonstrates high stability in passing through the intestinal barriers, which is essential for its absorption and utilization in the body. With these favorable characteristics, VMPL polypeptide holds great promise for future applications in the development of novel therapeutic agents and functional food ingredients aimed at improving glucose homeostasis and overall health.

• Rhessa Grace Guanga Ortizo, Vishal Sharma, Mei-Ling Tsai, Parushi Nargotra, Pei-Pei Sun, Chiu Wen Chen, Cheng-Di Dong, Integrating in silico, in vitro, and in situ approaches for characterization of novel peptides from tilapia (Oreochromis niloticus) viscera hydrolysates with dipeptidyl-peptidase IV inhibitory activity, Food Bioscience, Volume 63, 2025, 105619, ISSN 2212-4292, doi: org/10.1016/j.fbio.2024.105619.

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.