SV peptide

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

Batch to batch variation of the purity

• SVVYGLR polypeptide is a synthetic peptide with significant potential in promoting tissue regeneration, particularly in oral and maxillofacial regions.
• Derived from osteopontin, it exhibits angiogenic activity, comparable to that of potent angiogenic factors like VEGF. It induces the differentiation of fibroblasts into myofibroblasts and increases the expression of collagen type III. In vivo, it accelerates dermal and oral mucosal wound healing by enhancing cell motility and migratory activities of fibroblasts and keratinocytes.
• For skeletal muscle regeneration, it promotes cell motility of myogenic cells, facilitates their differentiation, and increases the efficiency of myotube formation. A single dose of this peptide shows potent utility in functional recovery of skeletal muscles after injury, with benefits such as increased muscle fiber diameter and reduced scar tissue formation.
• It likely functions through the TGF-β/Smad signaling pathway, and its short length and unique properties offer advantages like fast metabolism, lower immune response risk, and cost - effectiveness, with potential for developing more effective mutant peptides and various dosage forms.

• Tanaka S, Hamada Y, Yokoyama Y, Yamamoto H, Kogo M. Osteopontin-derived synthetic peptide SVVYGLR upregulates functional regeneration of oral and maxillofacial soft-tissue injury. Jpn Dent Sci Rev. 2021 Nov;57:174-181. doi: 10.1016/j.jdsr.2021.09.002. Epub 2021 Sep 28. PMID: 34630775; PMCID: PMC8487951.

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.