LRRKtide peptide

LRRKtide peptide

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

H-RLGRDKYKTLRQIRQ-OH

H-Arg-Leu-Gly-Arg-Asp-Lys-Tyr-Lys-Thr-Leu-Arg-Gln-Ile-Arg-Gln-OH

15

95.7%

C₈₃H₁₄₇N₃₁O₂₂

1931.24

Synthetic

Powder

LRRKtide is a peptide substrate for leucine-rich repeat kinase 2 (LRRK2). The sequence of LRRKtide has been derived from the ERM protein family members ezrin (amino acids 561-573), radixin (amino acids 558-570) and moesin (amino acids 539-553), proteins which influence cytoskeletal dynamics by anchoring the cytoskeleton to the plasma membrane. LRRK2 phosphorylates LRRKtide at its Thr558 site. LRRK2 is found in most organs and is involved in several cellular pathways. The LRRK2 gene and α-synuclein gene (SNCA) are the key influencing factors of Parkinson’s disease (PD), with dysfunction of LRRK2 influencing the accumulation of α-synuclein.

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

• Jaleel et al (2007) LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity. Biochem. J. 405 (2) 307 PMID: 17447891
• Anand and Braithwaite (2009) LRRK2 in Parkinson’s disease: biochemical functions. FEBS J. 276 6428 doi:10.1111/j.1742-4658.2009.07341.x
• Esteves et al (2014) LRRK2, a puzzling protein: Insights into Parkinson's disease pathogenesis. Exp. Neurol. 261 206 PMID: 24907399

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.