Cerecidin A1 peptide

Cerecidin A1 peptide

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

TTPLCVGVIIGLTTSIKICK

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

20

96.8%

Synthetic

Powder

There are thioether rings between residues 1-5 as well as 15-19. In addition, T2 and T13 are dehydrated (XXW2). It differs from A7 only at residues 12 and 14. Active against multiple Gram-positive strains, B. cereus As 1.348, B. cereus As 1.352, B. thuringiensis 1.1013, B. thuringiensis 1.1014, B. subtilis 1.107, B. subtilis DB104, B. pumilus 1.1165, E. faecalis 1.14, E. faecalis V583, E. durans 1.2023, E. pernyi 1.1010, L. coprophilus 1.214, L. acidophilus 100-33, L. casei 1.575, L. rhamnosus 1.104, L. plantarum 1.551, L. brevis 1.2028, L. brevis 1.7, L. buchneri 1.40, L. lactis LM0230, L. lactis MG1363, L. curvatus LTH1.174, L. dextranicum 181 (zone inhibition 6-10 mm, M. flavus NCIB8166 (zone inhibition 15 mm), S. bovis LG42, S. gordonii 1.2496, S. salivarius 1.2498, and S. thermophilus 1.1864 (Zone inhibition 7-9 mm), including resistant superbugs (MRSA and VRE). Cerecidin A1 was found in Bacillus cereus.

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

• Wang J, Zhang L, Teng K, Sun S, Sun Z, Zhong J. Cerecidins, novel lantibiotics from Bacillus cereus with potent antimicrobial activity. Appl Environ Microbiol. 2014;80(8):2633-43.

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.