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O-acyl bond incorporation technology
Increases peptide solubility, decreases aggregation
Powerful tool for β-amyloid research
Hydrophobic peptides are difficult to prepare and handle, making their study or use in biological research difficult. For example, β-amyloids, which are highly hydrophobic peptides, are prone to natural self-assembly. These peptides aggregate and deposit on organs, forming debilitating plaques that are involved in the progression of many neurodegenerative diseases such as Alzheimer's and Parkinson's, as well as other diseases such as diabetes and Huntington's. β-amyloids are targets for developing effective therapies to treat these diseases, but these studies are often hindered by uncontrollable aggregative nature of β-amyloids.
Our Click Peptides are synthesized using the O-acyl isopeptide method, which was developed by Taniguchi, et al (Figure 1). We use a special synthesis method to incorporate a strategically placed o-acyl bond in place of a naturally occurring n-acyl bond in the native peptide. The resulting peptide, called an o-acyl isopeptide, exhibits enhanced solubility and minimal peptide self-assembly, due to a reduction in intramolecular hydrogen bond interactions between peptide chains.
Adjusting the pH of the Click Peptide solution to ≥7.4 induces a rapid O→N intermolecular acyl migration (conversion of O-acyl bond to N-acyl bond), which rapidly converts the insoluble Click Peptide to its soluble native form. No byproduct is released when the Click Peptide is converted to the native peptide, making it advantageous for in vitro and in vivo biological experimental systems.
26-O-acyl β-amyloid (1-42) click peptide was successfully synthesized, the β-ester bond in which can be quickly and quantitatively converted to a native Gly25-Ser26 amide bond via a pH-dependent O-N intramolecular acyl migration reaction (t1/2 =1 min, pH 7.4, 37℃) at a hydroxyamino acid residue. Namely, upon this pH-triggered conversion (pH-click), the non-aggregative and water-soluble precursor (click peptide) can produce the monomer with a random-coil structure under physiological conditions (pH 7.4, 37℃). The structure information is as follows.
The following are HPLC reports of (Scheme 3) purified β-amyloid (1-42) native peptide converted from β-amyloid (1-42) click peptide (precursor) and (Scheme 4) purified 26-O-acyl β-amyloid (1-42) click peptide (precursor).
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