Temporin-SHd peptide

Temporin-SHd peptide

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

Batch to batch variation of the purity

FLPAALAGIGGILGKLF

Phe-Leu-Pro-Ala-Ala-Leu-Ala-Gly-Ile-Gly-Gly-Ile-Leu-Gly-Lys-Leu-Phe

17

95.9%

Synthetic

Powder

Structure and activity characterized by (Abbassi F et al 2012). Active against E. coli (MIC 5-50 uM depending on strains), A. baumannii (25 uM), S. aureus MRSA (6.25 uM), B. megaterium (1.56 uM), and S. cerevisiae (25 uM). Active against parasites L. infantum, L. major, L. tropica, L. amazonensis, L. braziliensis, L. infantum amastigotes Axenic, L. infantum amastigotes Intramacrophagic, T. brucei,and T. cruzi (IC50 6.7-23 uM). 50% hemolysis of human erythrocytes, Human THP-1 monocytes, and Human THP-1-derived macrophages at 44-66 uM. Updated 3/2014. Temporin-SHd was found in Pelophylax saharica, Africa.

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

• Abbassi F, Lequin O, Piesse C, et al. Temporin-SHf, a new type of phe-rich and hydrophobic ultrashort antimicrobial peptide. J Biol Chem. 2010;285(22):16880-92.

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.