Dermaseptin-S8 peptide

Dermaseptin-S8 peptide

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

H-ALWKTMLKKLGTVALHAGKAALGAAADTISQ-NH2

H-Ala-Leu-Trp-Lys-Thr-Met-Leu-Lys-Lys-Leu-Gly-Thr-Val-Ala-Leu-His-Ala-Gly-Lys-Ala-Ala-Leu-Gly-Ala-Ala-Ala-Asp-Thr-Ile-Ser-Gln-NH2

31

95.2%

C₁₄₁H₂₄₀N₄₀O₃₈S

3135.71

Synthetic

Powder

Dermaseptin sVIII has only one site of amino acid substitution when compared with dermaseptin sI. Unlike dermaseptin s1, mature dermaseptin sVI–sVIII peptides lacked the C-terminal tripeptide (-GE/AQ) of the precursor openreading frame deduced from their respective cDNAs. MS/ MS fragmentation of each peptide using a QTOF-Ultima instrument (Micromass, UK), established that each was C terminally amidated with either an isoleucine amide (sVI) or a glutamine amide (sVII–sVIII). The defensive skin secretions of frogs are known to contain a plethora of biologically active peptides, some of which share common primary structural features with endogenous vertebrate regulatory peptides and others that appear to have no obvious structural counterparts in higher vertebrates. The dermaseptins constitute a group of peptides that fall into the latter category displaying broad spectrum antimicrobial activity against both bacteria and fungi The role of this peptide family, typically consisting of 27–34 amino acid residues, is thought to be in defending the naked moist skin of the frogs against environmental or pathogenic microbial invasion. One must bear in mind that the integument of the amphibian plays many important physiological roles including respiration and osmoregulation—fundamental processes that could impinge upon the well-being of the animal if impaired by microbial colonisation. In fact, dermaseptins were the first vertebrate peptides to exhibit lethal effects against the filamentous fungi responsible for severe opportunistic infections accompanying immunodeficiency syndrome and the use of immunosuppressive agents.

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

• Chen T, Tang L, Shaw C. Identification of three novel Phyllomedusa sauvagei dermaseptins (sVI-sVIII) by cloning from a skin secretion-derived cDNA library. Regul Pept. 2003;116(1-3):139-46

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.