The preparation of hydrophobic peptides is a time consuming process. Even the peptides can be successfully prepared, proper dissolving of peptides poses a difficulty prior their assay experiments. For example, β-amyloid peptide, a typical hydrophobic peptide, is a target for developing effective therapies for treating Alzheimer's disease (AD). Recent studies often encounter obstacles because of the uncontrolled and aggregative features of β-amyloid. GenScript's featured click peptide service (SC1506) is designed to handle low water-solubility and aggregative nature of hydrophobic peptide.
- Service Features
- Principle
- Case Study
Key Features:
1. Control the following natures of the hydrophobic peptide
- Physicochemical property (e.g., water-solubility, self-assembly, aggregation, or folding).
- Biologic activity (e.g., ligand-receptor binding affinity, or enzyme-substrate binding affinity)
2. Convert to the native peptide (hydrophobic peptide) in situ by an exogenous action ("click")
- The "click peptide" (precursor) converts to native peptide easily at pH 7.4 or above.
- The conversion is a one way and quick process
- No by-product in the conversion process, suitable for biologic experiment
Key Advantages:
- Increase the solubility significantly in your research use
- Slow the aggregation dramatically
- Provide a novel system useful for investigating the dynamic biological functions of β-amyloid (1-42) in AD
- Applicable to cell signal transduction and other studies
References:
- 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
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A "click peptide" is a chemically-modified peptide precursor used to understand the biological function of peptides. The "click peptide" 1) does not exhibit the inherent biological activity of the original peptide due to a chemical modification of the peptide backbone and; 2) by adding an exogenous action ("click") such as pH-change, easily affords the native peptide in situ with a quick and easy one-way conversion via a native amide bond-forming reaction.
Our click peptide service uses the O-acyl isopeptide method which was developed by Atsuhiko Taniguchi, et al (Scheme 1). Hydrogen bond interactions between peptide chains often play a crucial role in the physicochemical and biologic actions through their contribution to the conformational stability of the higher order structure. The O→N intramolecular acyl migration is capable of rapid forming of amide bond under physiologic conditions (pH 7.4 or above) with an atom-economical reaction; thus, no byproduct is released during click peptide (precursor) converted to the native peptide, which is a great advantage in the toxicology in biologic experimental systems.
 Scheme 1: A click peptide based on the O-acyl isopeptide method 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
Result
- 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) |
Quotations and Ordering:
 For quotations, please use our Secure Instant Online Quotation/Order system. However, you may also contact us by email, phone (1-732-885-9188), fax (1-732-210-0262), or via our Secure Messaging System.
 Order can be placed by email, phone, or fax with either a PO (Purchase Order) or credit card. Please submit your peptide sequence at peptide@genscript.com using our Click Peptide Order Form. Our customer service representatives are available 24 hours, Monday through Friday to assist you.
We accept POs and major credit cards ( ). A 7% New Jersey sales tax will be applied to orders shipped to New Jersey. Your credit card will be billed under "GenScript USA Inc." Click here to download our credit reference form. For international orders, we must apply the full charge at the time the order is placed. In the unlikely event that any given order cannot be filled, our guarantee will take the form of a full refund.
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