Suc-Ala-Leu-Pro-Phe-pNA peptide

Suc-Ala-Leu-Pro-Phe-pNA peptide

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

Batch to batch variation of the purity

Suc-ALPF-pNA

Suc-Ala-Leu-Pro-Phe-pNA

4

95.28%

C₃₃H₄₂N₆O₉

666.72

128802-78-8

24860364

Synthetic

Powder

Suc-Ala-Leu-Pro-Phe-pNA (N-carboxypropionyl-Ala-Leu-Pro-Phe-p-nitroanilide) is a peptide substrate used to study the substrate specificity of the peptidyl prolyl cis-trans isomerase (PPI) activities of cyclophilin and the FK-506 binding protein (FKBP). Suc-Ala-Leu-Pro-Phe-pNA was found to be a more reactive substrate for FKBP compared to the standard PPI substrate, Suc-Ala-Ala-Pro-Phe-pNA. With this new substrate, the researchers were able to use lower concentrations of FKBP, allowing for more accurate determinations of Ki values for tight-binding inhibitors of FKBP.

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

• Harrison RK, Stein RL. Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes. Biochemistry. 1990 Apr 24;29(16):3813-6. doi: 10.1021/bi00468a001. PMID: 1693856.

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.