Dermcidin - DCD-1 peptide (TFA removed)

Dermcidin - DCD-1 peptide (TFA removed)

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-SSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVLDSV-OH

H-Ser-Ser-Leu-Leu-Glu-Lys-Gly-Leu-Asp-Gly-Ala-Lys-Lys-Ala-Val-Gly-Gly-Leu-Gly-Lys-Leu-Gly-Lys-Asp-Ala-Val-Glu-Asp-Leu-Glu-Ser-Val-Gly-Lys-Gly-Ala-Val-His-Asp-Val-Lys-Asp-Val-Leu-Asp-Ser-Val-OH

47

95.31%

C₂₀₄H₃₄₈N₅₆O₇₀

4705.25

Synthetic

Powder

DCD-1 is a 47-amino acid antimicrobial peptide (AMP). It is expressed in eccrine sweat glands, secreted into sweat at a concentration of 1-10µg/mL, and transported to the epidermal surface. Unlike most AMPs, which are cationic, DCD has a net negative charge. DCD-1 displays antimicrobial activity thereby limiting skin infection by potential pathogens in the first few hours after bacterial colonization. Highly effective against E.coli, E.faecalis, S.aureus and C.albicans. Optimal pH and salt concentration resemble the conditions in sweat. Also exhibits proteolytic activity. DCD-1 is able to bind to the cell surface but is not found in the bacterial cytoplasm. DCD-1L and DCD-1 are also active under high-salt conditions and in a buffer resembling human sweat.

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

• Steffen H, Rieg S, Wiedemann I, Kalbacher H, Deeg M, Sahl HG, Peschel A, Götz F, Garbe C, Schittek B. Naturally processed dermcidin-derived peptides do not permeabilize bacterial membranes and kill microorganisms irrespective of their charge. Antimicrob Agents Chemother. 2006 Aug;50(8):2608-20.

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.