Cytolysin peptide

Cytolysin peptide

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

Batch to batch variation of the purity

TTPACFTIGLGVGALFSAKFC

Thr-Thr-Pro-Ala-Cys-Phe-Thr-Ile-Gly-Leu-Gly-Val-Gly-Ala-Leu-Phe-Ser-Ala-Lys-Phe-Cys

21

95.8%

Synthetic

Powder

Enterococcus faecalis senses target cells and in response expresses cytolysin. The cytolysin consists of two structural subunits, CylLL and CylLS, that are activated by an extracellular protease, CylA. In the absence of target cells, the other subunit (CylL(L)'') forms a complex with CylL(S)'', blocking it from autoinducing the operon. When target cells are present, however, CylL(L)'' binds preferentially to the target, allowing free CylL(S)'' to accumulate above the induction threshold to express high levels of cytolysin (Coburn PS et al., 2004). The two chains work synergistically at a ratio of 1:1. CylLS contains two thioether bonds: T1-C5 and S17-C20. In addition, T2 and T7 are dehydrated. The AMINO ACID sequence of CylLL is TTPVCAVAATAAASSAACGWVGGGIFTGVTVWSLKHC. There are three thioether bonds: T1-C5, S14-C18, S34-C38. In addition, T2, T10, S15, and T30 are dehydrated. The peptide may also contain usual lanthionine stereochemistry (Tang and van der Donk, 2013 Nature Chem Biol ). Updated 1/2013; 9/2014. Cytolysin has Antimicrobial activity. The source of Cytolysin is Enterococcus faecalis.

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

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.