APP 17mer peptide (204-220AA of APP695)

APP 17mer peptide (204-220AA of APP695)

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

Ac-DDSDVWWGGADTDYADG-NH2

Ac-Asp-Asp-Ser-Asp-Val-Trp-Trp-Gly-Gly-Ala-Asp-Thr-Asp-Tyr-Ala-Asp-Gly-NH2

17

95.2%

C₈₁H₁₀₄N₂₀O₃₃

1885.79

Synthetic

Powder

APP 17mer peptide (204-220AA of APP695) is a 17–amino acid peptide corresponding to the GABA_BR1a(gamma-aminobutyric acid type B receptor subunit 1a) binding region within APP (Amyloid-beta precursor protein) suppressed in vivo spontaneous neuronal activity in the hippocampus of anesthetized Thy1-GCaMP6s mice. The sequence of APP 17mer peptide is: Ac-DDSDVWWGGADTDYADG-NH2. APP 17mer peptide could bind to sushi 1 domain of GABA_BR1a with a K_D of 810 nM, in the same ragne as the binding affinity of the entire linker region. APP 17-mer peptide mimics the effects of sAPPα on GABABR1a dependent inhibition of synaptic vesicle release. Also, APP 17-mer peptide suppresses neuronal activity of CA1 pyramidal cells 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

• Rice HC, de Malmazet D, Schreurs A, et al. Secreted amyloid-u03b2 precursor protein functions as a GABA_BR1a ligand to modulate synaptic transmission. Science. 2019;363(6423)

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.