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.
Click Peptide Service
- Service Features
- Case Study
Key Features 1. Click Peptide Synthesis allows control over
2. Control over Click Peptide to native peptide conversion
- Physicochemical peptide properties (e.g., water-solubility, self-assembly, aggregation, or folding)
- Biologic activities (e.g., ligand-receptor binding affinity, or enzyme-substrate binding affinity)
- Click peptide converts to native peptide easily at pH 7.4 or above
- Conversion is a one-way, quick process
- No by-product formation during conversion, suitable for biological experiments
- Increases peptide solubility
- Slows peptide aggregation
- Novel system useful for investigating the dynamic biological functions of β-amyloids in neurodegenerative diseases and other diseases exhibiting amyloidosis
- Atsuhiko Taniguchi, Youhei Sohma, et al. Click peptide: Chemical Biology-oriented analogues of Alzheimer's amyloid β peptide 1–42. J. Peptide Science. Nov 2006; 12(12): 823-828
- Youhei Sohma, Atsuhiko Taniguchi, et al. Controlled Production of Amyloid β Peptide from a Photo-Triggered, Water-Soluble Precursor "Click Peptide". ChemBioChem. Nov 2008; 9(18): 3055-3065
- Hui Wang, Taeko Kakizawa, et al. Synthesis of amyloid β peptide 1–42 (E22Δ) click peptide: pH-triggered in situ production of its native form. Bioorganic & Medicinal Chemistry. July 2009; 17(14): 4881-4887
- Taniguchi A, Kiso Y, et al. "Click peptide": pH-triggered in situ production and aggregation of monomer Abeta1-42. ChemBioChem. Mar 2009; 10(4): 710-715
- Claudia Balducci, Marten Beeg, et al. Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein. PNAS. Jan 2010; doi:10.1073
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.
Figure 1: Conversion of Click Peptide to native peptide via pH change
Reference Atsuhiko Taniguchi, Youhei Sohma, et al. Click peptide: Chemical Biology-oriented analogues of Alzheimer's amyloid β peptide 1–42. J. Peptide Science. Nov 2006; 12(12): 823-828
|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.|
Scheme 2: β-amyloid (1-42) click peptide
- β-amyloid precursor(click peptide) has a water solubility of 15 mg/ml, while it is only 0.14 mg/ml for the native peptide.
- The aggregative property of the peptides reduced significantly.
- The O-acyl moiety was stable under acidic pH.
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).
(Scheme 3) HPLC report of purified β-amyloid (1-42) native peptide converted from β-amyloid (1-42) click peptide (precursor)
(Scheme 4) HPLC report of purified 26-O-acyl β-amyloid (1-42) click peptide (precursor)
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