biomineralization-directing peptide

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

Batch to batch variation of the purity

• MLPHHGA peptide is a heptapeptide with unique properties and significant potential in biomaterials and tissue engineering applications. It is designed to direct the mineralization process, specifically the formation of hydroxyapatite.
• This peptide is incorporated at the C-terminal of MDG1, where it can be displayed from the fibril surface. It has been shown to have a notable impact on mineral formation. MLPHHGA slows the mineralization rate and accelerates the transformation of amorphous calcium phosphate (ACP) into crystalline octacalcium phosphate (OCP), resulting in the formation of elongated, plate-like particles. The presence of this peptide in MDG1 hydrogels allows for better control over the morphology and phase of the deposited calcium phosphate mineral, with the ability to form highly crystalline and elongated structures resembling biological apatite. Overall, MLPHHGA peptide offers a valuable tool for guiding biomineralization processes and holds great promise in the development of functional biomaterials for applications such as bone tissue engineering.

• Gungormus M, Branco M, Fong H, Schneider JP, Tamerler C, Sarikaya M. Self assembled bi-functional peptide hydrogels with biomineralization-directing peptides. Biomaterials. 2010 Oct;31(28):7266-74. doi: 10.1016/j.biomaterials.2010.06.010. Epub 2010 Jun 29. PMID: 20591477; PMCID: PMC4120958.

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.