PPF-BBI peptide

PPF-BBI peptide

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

H-ALRGCWTKSIPPKPCP-NH2

H-Ala-Leu-Arg-Gly-Cys-Trp-Thr-Lys-Ser-Ile-Pro-Pro-Lys-Pro-Cys-Pro-NH2

16

95.2%

C₇₉H₁₂₉N₂₃O₁₈S₂

1753.14

Synthetic

Powder

PPF-BBI is a novel bioactive Bowman-Birk type inhibitory hexadecapeptide of the Ranacyclin family from the defensive skin secretion of the Fukien gold-striped pond frog, Pelophlax plancyi fukienesis. PPF-BBI was shown to possess a potent trypsin and tryptase inhibitory activity with a high specificity. A better antimicrobial activity was observed when P16 of PPF-BBI was replaced by Lys, and the addition of the cell-penetrating peptide Tat48–56 resulted in a peptide with a strong antifungal activity. The specificity of inhibition is determined by whether the P1 position residue can fit into the S1 pocket of protease. Based on previous reports, Lys as the P1 position is optimal for trypsin inhibition, and Phe is optimal for chymotrypsin. Similarly, PPF-BBI, which has a Lys at the P1 site, showed a strong trypsin inhibitory activity and substitution of the Lys at the P1 position, with Phe leading to the elimination of the trypsin inhibition and giving rise to a chymotrypsin inhibitory activity. In the tryptase activity assay, PPF-BBI displayed a mild potency toward tryptase with a Ki value of 30.52 µM. K16-PPF-BBI shows a three-fold better inhibition with a Ki value of 9.67 µM

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

• Miao Y, Chen G, Xi X, et al. Discovery and Rational Design of a Novel Bowman-Birk Related Protease Inhibitor. Biomolecules. 2019;9(7)

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.