Liraglutide peptide (TFA removed)

Liraglutide 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

HAEGTFTSDVSSYLEGQAAK(gamma-Glu-palmitoyl)EFIAWLVRGRG

His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys(palm-gama-Glu)-Glu-Phe-Ile-Ala-Trp-Leu-Val-Arg-Gly-Arg-Gly

31

98.05%

C₁₇₂H₂₆₅N₄₃O₅₁

3751.2

Synthetic

Powder

Liraglutide, the second GLP-1 analog approved in 2009 in Europe and 2010 in USA under the trade name Victoza (Novo Nordisk). Liraglutide is a synthetic molecule produced using DNA recombinant technology. Compared to native GLP-1, it has an addition of a 16 carbon fatty-acid side-chain at Lys26 and an Arg34Lys substitution (Neumiller et al., 2010). After s.c. injection, only 1–2% of liraglutide circulates as free peptide in the plasma as the rest is noncovalently bound to albumin as ensured by the fatty acid side-chain (Zhang et al., 2012). This prolongs the half-life of liraglutide to 11–15 h approximately and hence administration once daily is needed.

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

• Malm-Erjefalt M, Bjornsdottir I, Vanggaard J, Helleberg H, Larsen U, Oosterhuis B, van Lier JJ, Zdravkovic M, Olsen AK: Metabolism and excretion of the once-daily human glucagon-like peptide-1 analog liraglutide in healthy male subjects and its in vitro degradation by dipeptidyl peptidase IV and neutral endopeptidase. Drug Metab Dispos. 2010 Nov;38(11):1944-53. doi: 10.1124/dmd.110.034066. Epub 2010 Aug 13.

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.