Dentonin peptide

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

Batch to batch variation of the purity

Dentonin, also known as AC-100, is a synthetic peptide corresponding to the central fragment (residues 242-264) of Matrix Extracellular Phosphoglycoprotein (MEPE). This peptide contains an integrin-binding RGD sequence (residues 247-249), a glycosaminoglycan-attachment SGDG motif (residues 256-259), and a putative calcium-binding domain. Dentonin has been shown to stimulate the proliferation of human bone marrow stromal cells and promote their differentiation into osteoblast precursors. The peptide exhibits biological activity in both in vitro and in vivo settings, where it enhances new bone formation.

MEPE, a member of the SIBLING family (Small Integrin-Binding LIgand, N-linked Glycoprotein), is involved in bone and dentin mineralization processes. Dentonin's functional domains, including the RGD and SGDG sequences, contribute to its interaction with cellular and extracellular components, influencing cell adhesion and signaling pathways. Studies indicate that Dentonin plays a role in early cellular events, such as progenitor cell recruitment and proliferation, though its effects on terminal differentiation and mineralization remain less pronounced.

• Six N, Septier D, Chaussain-Miller C, Blacher R, DenBesten P, Goldberg M. Dentonin, a MEPE fragment, initiates pulp-healing response to injury. J Dent Res. 2007 Aug;86(8):780-5. doi: 10.1177/154405910708600818. PMID: 17652210.

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.