PTD2 peptide

PTD2 peptide

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

Batch to batch variation of the purity

Ac-GVXRI-NH2, X is Nle

Ac-Gly-Val-Nle-Arg-Ile-NH2

5

95.3%

C₂₇H₅₁N₉O₆

597.76

Synthetic

Powder

PTD2 is a peptide derived from the histone H4 sequence surrounding residue K44 (H4K44) that acts as an inhibitor of Wolf-Hirschhorn syndrome candidate 1 (WHSC1). WHSC1 (also known as NSD2 or MMSET) is a histone 3 lysine 36 (H3K36) specific methyltransferase that is responsible for mono- and dimethylation of lysine 36 on histone H3, and is frequently deleted in the genetic disorder Wolf-Hirschhorn syndrome, and has also been implicated as a driver in a variety of haematological and solid tumours. PTD2 inhibits WHSC1 in biochemical and biophysical assays with similar micromolar potencies, but demonstrates no enzymatic inhibition against a panel of other histone methyltransferases. PTD2 is a valuable tool for in vitro assay development and validation.

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

• Morrison et al (2018) Identification of a peptide inhibitor for the histone methyltransferase WHSC1. PLoS One 13(5) PMID: 29742153

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.