HAV peptide

HAV peptide

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

Batch to batch variation of the purity

H-HAV-OH

H-His-Ala-Val-OH

3

95.79%

C₁₄H₂₃N₅O₄

325.36

Synthetic

Powder

HAV polypeptide, a mimetic of the N - cadherin (NCad) adhesive interface, is designed to regulate mesenchymal stem cell (MSC) chondrogenesis. Incorporated into hyaluronic acid (HA) hydrogels, it enables precise control of cell - cell signaling. By varying the peptide concentration, it shows a dose - dependent enhancement of early chondrogenic gene expression and long - term cartilage matrix production. For example, at the highest dose of 2 × 10⁻³ M, type II collagen and glycosaminoglycan production significantly increase.
The peptide also features an ADAM10 - cleavable domain, allowing for the study of the timing and duration of its presentation. When cleavage is inhibited by a small - molecule ADAM10 inhibitor, chondrogenesis is restored, highlighting the importance of its stable presentation for MSC chondrogenesis. Overall, the HAV polypeptide offers a valuable tool for tissue engineering applications, particularly in cartilage repair and regeneration, by emulating the dynamic cell - cell interactions crucial for embryogenesis.

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

• Kwon MY, Vega SL, Gramlich WM, Kim M, Mauck RL, Burdick JA. Dose and Timing of N-Cadherin Mimetic Peptides Regulate MSC Chondrogenesis within Hydrogels. Adv Healthc Mater. 2018 May;7(9):e1701199. doi: 10.1002/adhm.201701199. Epub 2018 Jan 23. PMID: 29359863; PMCID: PMC6296766.

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.