Tat-beclin 1 peptide

Tat-beclin 1 peptide

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

Batch to batch variation of the purity

H-YGRKKRRQRRRGGTNVFNATFEIWHDGEFGT-OH

H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Gly-Gly-Thr-Asn-Val-Phe-Asn-Ala-Thr-Phe-Glu-Ile-Trp-His-Asp-Gly-Glu-Phe-Gly-Thr-OH

31

95.26%

C₁₆₄H₂₅₁N₅₇O₄₅

3741.08

Synthetic

Powder

Tat-beclin 1 is a cell permeable peptide derived from the domain of the autophagy protein beclin 1 that interacts with HIV-1 Nef, attached to the HIV-1 Tat protein transduction domain. Tat-beclin 1 activates beclin1 by competing against its negative regulator GAPR-1/glioma pathogenesis-related protein-2 (GLIPR2). Tat-beclin 1 suppresses the accumulation of htt103Q, a polyglutamine expansion protein derived from human mutant Huntingtin protein, and can inhibit the replication of pathogens including HIV-1 and West Nile virus in vitro and in vivo.

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

• Shoji-Kawata et al (2013) Identification of a candidate therapeutic autophagy-inducing peptide. Nature 494(7436) 201 PMID: 23364696
• Maejima (2016) Regulation of autophagy by Beclin 1 in the heart. J Mol Cell Cardiol 95 19 PMID: 26546165
• Wong (2019) Intestinal epithelial tight junction barrier regulation by autophagy-related protein ATG6/beclin 1. Am J Physiol Cell Physiol. 316(5) C753 PMID: 30892937

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.