Thanatin peptide (TFA removed)

Thanatin peptide (TFA removed)

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

Batch to batch variation of the purity

GSKKPVPIIYCNRRTGKCQRM

H-Gly-Ser-Lys-Lys-Pro-Val-Pro-Ile-Ile-Tyr-Cys-Asn-Arg-Arg-Thr-Gly-Lys-Cys-Gln-Arg-Met-OH (disulfide bond: Cys¹¹-Cys¹⁸)

21

98.57%

C₁₀₃H₁₇₇N₃₅O₂₇S₃

2433.9

16143622

Synthetic

Powder

Thanatin is an inducible 21-residue cationic antimicrobial peptide that was first isolated from the hemolymph of the hemipteran insect Podisus maculiventris (spined soldier bug), through immune challenge. Thanatin is strongly cationic (pI of 10.48) and contains a distinct short eight-residue basic loop created through a disulfide bond formation between residues Cys11 and Cys18 at the C-terminus. Thanatin exerts bactericidal activity by disrupting outer membrane(OM) integrity. Thanatin damages the OM by promoting the release of divalent cations. Thanatin competitively replaces the divalent cations to bind to LPS, thereby disrupting the integrity of OM and leading to bacterial death.

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

• Ma, B., Fang, C., Lu, L. et al. The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase. Nat Commun 10, 3517 (2019).
• Dash R, Bhattacharjya S. Thanatin: An Emerging Host Defense Antimicrobial Peptide with Multiple Modes of Action. Int J Mol Sci. 2021 Feb 3;22(4):1522. doi: 10.3390/ijms22041522. PMID: 33546369; PMCID: PMC7913509.

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.