Decoralin-NH2 peptide

Decoralin-NH2 peptide

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

H-SLLSLIRKLIT-NH2

H-Ser-Leu-Leu-Ser-Leu-Ile-Arg-Lys-Leu-Ile-Thr-NH2

11

95.79%

C₅₈H₁₁₀N₁₆O₁₄

1255.59

Synthetic

Powder

These factors are present in decoralin-NH2, but not in decoralin, which as a consequence, led to the lower helical content of decoralin than decoralin-NH2. However, when comparing decoralin versus anoplin, both in the amidated form, other structural features should be taken into account for this case. These features are principally related to the average hydrophobicity and hydrophobic moment, and the angle subtended by their polar faces. Anoplin presents a lower mean hydrophobic moment and mean hydrophobicity and higher polar angle than decoralin, these parameters would contribute to its lower helical content in the zwitterionic and in anionic vesicles compared to the decoralins. Moreover, these parameters taken together can also be correlated to the enhanced biological activities of decoralin-NH2 in relation to anoplin.

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

• Konno, Katsuhiro et al. “Decoralin, a novel linear cationic alpha-helical peptide from the venom of the solitary eumenine wasp Oreumenes decoratus.” Peptides vol. 28,12 (2007): 2320-7.

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.