hCDR1 peptide (TFA removed)

hCDR1 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-GYYWSWIRQPPGKGEEWIG-OH

H-Gly-Tyr-Tyr-Trp-Ser-Trp-Ile-Arg-Gln-Pro-Pro-Gly-Lys-Gly-Glu-Glu-Trp-Ile-Gly-OH

19

97.27%

C₁₁₁H₁₄₉N₂₇O₂₈

2309.57

Synthetic

Powder

Peptide hCDR1 is a potential candidate for a novel specific treatment of systemic lupus erythematosus (SLE) patients. It is based on the complementarity determining region (CDR)1 of a human monoclonal anti-DNA autoantibody. The peptide has been shown to either prevent or treat an already established murine lupus in SLE-prone mice or in mice with induced experimental SLE. In the present study, it was tested for its therapeutic potential in a model of lupus in severe combined immunodeficient (SCID) mice engrafted with peripheral blood lymphocytes (PBL) of patients with SLE. The peptide was found to significantly down-regulate the levels of dsDNA-specific antibodies and ameliorate the clinical features manifested by proteinuria, human IgG complex deposits as well as deposits of murine complement C3.

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

• Mauermann N, Sthoeger Z, Zinger H, Mozes E. Amelioration of lupus manifestations by a peptide based on the complementarity determining region 1 of an autoantibody in severe combined immunodeficient (SCID) mice engrafted with peripheral blood lymphocytes of systemic lupus erythematosus (SLE) patients. Clin Exp Immunol. 2004 Sep;137(3):513-20. doi: 10.1111/j.1365-2249.2004.02559.x. PMID: 15320900; PMCID: PMC1809128.

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.