P08 peptide

P08 peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

NMA-IEALFQGPPK(DNP)FR

NMA-Ile-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Pro-Lys-DNP-Phe-Arg-OH

12

95.47%

C₈₁H₁₁₂N₂₀O₂₁

1701.91

Synthetic

Powder

The peptide P08, with the sequence NMA-IEALFQGPPK(DNP)FR, is a fluorogenic peptide substrate that was determined to be the most efficiently cleaved by EV71 3C protease. It has a kinetic constant kcat / Km of 11.8 ± 0.82 mM⁻¹ min⁻¹. The substrate specificity study revealed that EV71 3C protease showed strong preference for the P2 and P1' residues of P08. Variants at these positions dramatically reduced the cleavage efficiency by the protease. Molecular dynamics simulations suggested that Arg39, located at the bottom of the S2 pocket of EV71 3C protease, may assist the process of cleavage of the substrate by interacting with the Phe residue at the P2 position of P08. P08 is an ideal substrate for biochemical characterization of EV71 3C protease and for the development of a biochemical assay for screening EV71 3C protease inhibitors. NMA=2-(N-methylamino)benzoyl. λex=340 nm and λem=440 nm for NMA/DNP.

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

• Shang L, Zhang S, Yang X, Sun J, Li L, Cui Z, He Q, Guo Y, Sun Y, Yin Z. Biochemical characterization of recombinant Enterovirus 71 3C protease with fluorogenic model peptide substrates and development of a biochemical assay. Antimicrob Agents Chemother. 2015 Apr;59(4):1827-36. doi: 10.1128/AAC.04698-14. Epub 2014 Nov 24. PMID: 25421478; PMCID: PMC4356770.

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.