Pinipesin peptide

Pinipesin peptide

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

Batch to batch variation of the purity

H-VAEARQGSFSY-OH

H-Val-Ala-Glu-Ala-Arg-Gln-Gly-Ser-Phe-Ser-Tyr-OH

11

95.2%

C₅₃H₇₉N₁₅O₁₈

1214.28

Synthetic

Powder

Pinipesin is a novel antimicrobial peptide, present in the exuviae extract of the centipede Scolopendra subspinipes subspinipes. Pinipesin displayed potent antimicrobial effects against different microorganisms and showed low haemolytic effects against human erythrocytes at high concentrations. Its sequence exhibited high similarity with some cuticular proteins, and it might act intracellularly by interfering with protein synthesis. Pinipesin might be part of a prophylactic immune response during the ecdysis process of centipedes. Pinipesin is sensitive to plasma proteases – almost totally digested within 60 min.

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

• Chaparro-Aguirre E, Segura-Ramu00edrez PJ, Alves FL, Riske KA, Miranda A, Silva Ju00fanior PI. Antimicrobial activity and mechanism of action of a novel peptide present in the ecdysis process of centipede Scolopendra subspinipes subspinipes. Sci Rep. 2019;9(1):13631

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.