Beta-defensin 3 peptide

Beta-defensin 3 peptide

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

Batch to batch variation of the purity

H-GIINTLQKYYCRVRGGRCAVLSCLPKEEQIGKCSTRGRKCCRRKK-OH
(Disulfide bridge: 11-40, 18-33, 23-41)

H-Gly-Ile-Ile-Asn-Thr-Leu-Gln-Lys-Tyr-Tyr-Cys-Arg-Val-Arg-Gly-Gly-Arg-Cys-Ala-Val-Leu-Ser-Cys-Leu-Pro-Lys-Glu-Glu-Gln-Ile-Gly-Lys-Cys-Ser-Thr-Arg-Gly-Arg-Lys-Cys-Cys-Arg-Arg-Lys-Lys-OH

45

95.2%

C₂₁₆H₃₇₁N₇₅O₅₉S₆

5155.09

Synthetic

Powder

This is a 5.1kDa 45-amino acid antimicrobial peptide called beta-Defensin-3 (hBD-3) having a beta sheet with three intramolecular disulfide bonds. It is expressed in high levels in keratinocytes and tonsilar tissue while expressed low in epithelia of the respiratory, gastrointestinal and genito-urinary tracts. Factors that induce its expression include TNF-alpha, IL-1beta and bacteria such as P. aeruginosa and S. aureus. hBD-3 is also potentially induced after exposure to IFN-gamma. In contrast to hBD-1, -2 and -4, hBD-3 demonstrates a salt-insensitive antimicrobial activity towards several pathogenic microorganisms at physiologic salt concentrations. This makes hBD-3 uniquely and particularly relevant in diseases where other hBDs show inactivity. The ability of hBD-3 to elicit its antimicrobial activity more effectively at the concentrations lower that those of hBD-1 and hBD-2 has been attributed to its amphipathic dimer structure and the increased positive surface charge (+9), compared to hBD-1 (+4) and hBD-2 (+6). hBD-3 has been shown to induce cytokine production from human keratinocytes and stimulates monocyte migration.

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

• J. Harder, J. Bartels, E. Christophers, and J.-M. Schröder, J. Biol. Chem., 276, 5707 (2001). (Original);
• L.A. Duits, et al., Biochem. Biophys. Res. Commun., 280, 522 (2001). (Pharmacol.);
• H.P. Jia, et al., Gene, 263, 211 (2001).

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.