Tachyplesin-1/TP-1 peptide

Tachyplesin-1/TP-1 peptide

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

Batch to batch variation of the purity

H-KWCFRVCYRGICYRRCR-NH2

H-Lys-Trp-Cys-Phe-Arg-Val-Cys-Tyr-Arg-Gly-Ile-Cys-Tyr-Arg-Arg-Cys-Arg-NH2

17

95.58%

C₉₉H₁₅₁N₃₅O₁₉S₄

2263.73

Synthetic

Powder

Tachyplesin-1 or TP-1 (KWCFRVCYRGICYRRCR-NH2) is a well characterized, structurally and mechanistically, AMP from the hemocyte of horse shoe crab. TP-1 has a broad spectrum of antimicrobial activity against several strains of Gram-negative and Gram-positive bacteria, fungi and viruses. The antimicrobial activity of TP-1 appears to stem from the ability of the peptide to disorganize bacterial cell membranes. NMR studies demonstrated that TP-1 adopts β-hairpin structure in solution and also in lipid micelles and bilayers. The antiparallel β-strands of β-hairpin structure of TP-1 are constrained by the disulfide bridges between residues Cys3–Cys16 and Cys7–Cys12

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

• Saravanan R, Mohanram H, Joshi M, Domadia PN, Torres J, Ruedl C, Bhattacharjya S. Structure, activity and interactions of the cysteine deleted analog of tachyplesin-1 with lipopolysaccharide micelle: Mechanistic insights into outer-membrane permeabilization and endotoxin neutralization. Biochim Biophys Acta. 2012 Jul;1818(7):1613-24. doi: 10.1016/j.bbamem.2012.03.015. PMID: 22464970.

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.