MARCKS-ED peptide

MARCKS-ED peptide

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

Batch to batch variation of the purity

H-KKKKKRFSFKKSFKLSGFSFKKNKK-OH

H-Lys-Lys-Lys-Lys-Lys-Arg-Phe-Ser-Phe-Lys-Lys-Ser-Phe-Lys-Leu-Ser-Gly-Phe-Ser-Phe-Lys-Lys-Asn-Lys-Lys-OH

25

95.15%

C₁₄₇H₂₄₃N₄₁O₃₁

3080.75

Synthetic

Powder

MARCKS-ED is a 25-mer peptide derived from the effector domain of the intracellular membrane protein myristoylated alanine-rich C-kinase substrate. MARCKS-ED can recognize phosphatidylserine (PS) with a preference for highly curved vesicles in a sequence specific manner. In synthetic lipid vesicles, it preferentially binds to highly curved vesicles containing PS, as shown by cosedimentation assays and fluorescence enhancement and anisotropy assays. In complex biological systems, it can detect highly curved, PS-enriched extracellular vesicles in rat plasma and specifically bind to PS-exposing membranes in a C. elegans model, suggesting its ability to sense both shape and lipid composition of membranes. MARCKS-ED could become a prototype for a new generation of peptide sensors that can simultaneously detect both PS and curvature. It may facilitate investigations of critical biological events such as extracellular vesicles shedding and apoptosis, and potentially serve as a small peptide alternative to Annexin V in detecting PS-exposing membranes in live animals.

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

• Morton LA, Yang H, Saludes JP, Fiorini Z, Beninson L, Chapman ER, Fleshner M, Xue D, Yin H. MARCKS-ED peptide as a curvature and lipid sensor. ACS Chem Biol. 2013 Jan 18;8(1):218-25. doi: 10.1021/cb300429e. Epub 2012 Oct 29. PMID: 23075500; PMCID: PMC3548944.

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.