ATI 2341 peptide

ATI 2341 peptide

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

Palmitolyl-MGYQKKLRSMTDKYRL-OH

Palmitolyl-Met-Gly-Tyr-Gln-Lys-Lys-Leu-Arg-Ser-Met-Thr-Asp-Lys-Tyr-Arg-Leu-OH

16

95.65%

C₁₀₄H₁₇₈N₂₆O₂₅S₂

2256.81

Synthetic

Powder

ATI 2341 is a pepducin targeting the C-X-C chemokine receptor type 4 (CXCR) at which it is an allosteric agonist with an EC50 of 194 nM. ATI 2341 functions as a biased ligand, favouring Gαi activation over Gα13. In contrast to the the natural CXCR4 agonist, stromal cell-derived factor-1α, ATI 2341 does not promote β-arrestin recruitment. ATI 2341 induces chemotaxis in CXCR4 expressing cells in vitro and acts as a functional antagonist to mobilise polymorphonuclear neutrophils and hematopoietic stem and progenitor cells from bone marrow niche in both mice and non-human primates.

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

• Tchernychev et al (2010) Discovery of a CXCR4 agonist pepducin that mobilizes bone marrow hematopoietic cells. Proc.Natl.Acad.Sci.U.S.A. 107 22255 PMID: 21139054
• Quoyer et al (2013) Pepducin targeting the C-X-C chemokine receptor type 4 acts as a biased agonist favoring activation of the inhibitory G protein. Proc.Natl.Acad.Sci.U.S.A. 110 E5088 PMID: 24309376
• Planesas et al (2015) Studying the binding interactions of allosteric agonists and antagonists of the CXCR4 receptor. J.Mol.Graph Model. 60 1 PMID: 26080355

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.