HAVDI peptide

HAVDI peptide

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

Batch to batch variation of the purity

Fmoc-HAVDI-OH

Fmoc-His-Ala-Val-Asp-Ile-OH

5

95.68%

C₃₉H₄₉N₇O₁₀

775.84

Synthetic

Powder

HAVDI polypeptide, a synthetic peptide engineered to mimic the functional properties of the N - cadherin protein, is designed with a precise sequence to actively interact with cells and modulate their behavior. This peptide exhibits the remarkable ability to self - assemble into nanofibrous structures, thereby creating a three - dimensional scaffold that bears a striking resemblance to the natural extracellular matrix (ECM). This scaffold not only offers essential physical support to cells but also plays a crucial role in guiding their growth, adhesion, and proliferation processes.
The specifically designed N - cadherin mimetic peptides, namely Fmoc - HAVDI and Nap - HAVDI, exemplify this self - assembly property. At physiological pH, they spontaneously form a nanofibrous network, which gives rise to a bioactive peptide hydrogel. The nanofibrous network within these pentapeptide hydrogels closely mimics the topology of the natural ECM, and interestingly, the mechanical strength of the gels precisely matches that of the native ECM of neural cells. This unique combination of properties enables the hydrogels to effectively support cell adhesion and proliferation of both neural and non - neural cell lines, thus highlighting the versatility and adaptability of these peptidic scaffolds.
In the realm of tissue engineering, HAVDI polypeptide has emerged as a highly promising candidate. It actively promotes cell - cell interactions, a fundamental process for tissue regeneration. Its biocompatibility with a diverse range of cell types, including both neural and non - neural cells, is a significant advantage, ensuring minimal cytotoxicity and maximizing its potential for use in vivo. This peptide's distinctive characteristics render it an invaluable tool for in - depth studies of cell behavior and for the development of novel, innovative therapies in the field of regenerative medicine. By leveraging its properties, it becomes possible to engineer functional tissues and organs, opening up new avenues and possibilities for the treatment of a wide spectrum of diseases and injuries. Moreover, the tunable nature of the HAVDI polypeptide allows for customization to meet the specific requirements of different applications, further augmenting its versatility and effectiveness in various biomedical contexts.

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

• Kaur H, Roy S. Designing aromatic N-cadherin mimetic short-peptide-based bioactive scaffolds for controlling cellular behaviour. J Mater Chem B. 2021 Aug 7;9(29):5898-5913. doi: 10.1039/d1tb00598g. Epub 2021 Jul 15. PMID: 34263278.

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.