SMRwt peptide

SMRwt peptide

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

Batch to batch variation of the purity

H-VGFPVAAVGFPVDYKDDDDK-OH

H-Val-Gly-Phe-Pro-Val-Ala-Ala-Val-Gly-Phe-Pro-Val-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-OH

20

95.77%

C₉₉H₁₄₄N₂₂O₃₂

2154.32

Synthetic

Powder

SMRwt is derived from the secretion modification region (SMR, amino acids 66 to 70) of the HIV-1 Nef protein. Nef is a 27-kDa protein produced early during HIV infection of a cell, which interacts with mortalin, a member of the heat shock 70-kDa protein family via Nef's SMR motif, an interaction which is disrupted by the SMRwt peptide. In breast cancer cells SMRwt interacts with mortalin and also the structural protein vimentin to inhibit pro-epithelial-mesenchymal transition (EMT) exosome release, and induce EMT tumour suppressor protein expression. Exosomes containing EMT programs transmit pro-metastatic phenotypes and SMRwt peptide treatment results in an effective blockade of breast cancer cell migration.

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

• Shelton et al (2012) Secretion modification region-derived peptide disrupts HIV-1 Nef's interaction with mortalin and blocks virus and Nef exosome release. J Virol. 86(1) 406 PMID: 22013042
• Huang et al (2017) Secretion modification region-derived peptide blocks exosome release and mediates cell cycle arrest in breast cancer cells. Oncotarget 8(7) 11302 PMID: 28076321
• Huang et al (2022) Novel secretion modification region (SMR) peptide exhibits anti-metastatic properties in human breast cancer cells. Sci Rep. 12(1) 13204 PMID: 35915218

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.