Dermcidin - DCD-1L peptide

Dermcidin - DCD-1L peptide

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

Batch to batch variation of the purity

H-SSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVLDSVL-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-Leu-OH

48

97.54%

C₂₁₀H₃₅₉N₅₇O₇₁

4818.41

Synthetic

Powder

DCD-1L is a dermcidin-derived peptide. It is constitutively expressed in eccrine sweat glands and secreted into sweat. It has an amino acid sequence of SSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVLDSVL with a net charge of -2 and a calculated pI of 5.07. DCD-1L shows antimicrobial activity against a variety of pathogenic microorganisms including Staphylococcus aureus, Escherichia coli, Enterococcus faecalis, Candida albicans, Staphylococcus epidermidis, Pseudomonas putida, methicillin-resistant S. aureus, rifampin- and isoniazid-resistant Mycobacterium tuberculosis, Listeria monocytogenes, and Salmonella enterica serovar Typhimurium. It is proteolytically processed from a 110-amino-acid precursor protein of dermcidin. In human eccrine sweat, DCD-1L and other DCD-derived peptides are generated by postsecretory proteolytic processing, and its activity may be related to the formation of stable complexes and interaction with the bacterial membrane, although it does not permeabilize the bacterial membrane like some other antimicrobial peptides. The alteration from anionic DCD-1L to cationic peptides during proteolytic processing may lead to a different spectrum of antimicrobial activity, and at least the first three amino acids SSL seem important for its antimicrobial function, with the active part of its sequence potentially residing in the first 23 amino acids.

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

• Schittek B, Hipfel R, Sauer B, et al. Dermcidin: a novel human antibiotic peptide secreted by sweat glands. Nat Immunol. 2001;2(12):1133-7.

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.