Synthetic peptides, pharmaceutical compositions containing synthetic peptides, and the use of synthetic peptides for the treatment of amyloidosis.
A synthetic peptide targeting amyloid proteins inhibits their aggregation and maintains cell viability, addressing the inefficacies of conventional treatments for amyloidosis.
Patent Information
- Authority / Receiving Office
- JP · JP
- Patent Type
- Applications
- Current Assignee / Owner
- CHINA MEDICAL UNIV HOSPITAL
- Filing Date
- 2025-01-24
- Publication Date
- 2026-05-19
AI Technical Summary
Conventional treatments for amyloidosis, such as Alzheimer's and Parkinson's diseases, suffer from side effects and insufficient efficacy, necessitating the development of novel drugs with high efficacy.
A synthetic peptide with a specific amino acid sequence (SEQ ID NO: 1) is designed to target and inhibit the formation and aggregation of amyloid proteins, including beta-amyloid, tau protein, alpha-synuclein, islet amyloid polypeptide, and transthyretin, maintaining cell viability and preventing amyloid aggregation.
The synthetic peptide effectively inhibits amyloid aggregation and maintains cell viability, demonstrating a dose-dependent inhibitory effect on amyloid formation in neuronal cells, thereby treating amyloidosis.
Smart Images
Figure 2026082598000001_ABST
Abstract
Description
[Technical Field]
[0001] The present invention relates to synthetic peptides, pharmaceutical compositions containing synthetic peptides, and the use of synthetic peptides for treating amyloidosis. [Background technology]
[0002] Amyloid is an insoluble fibrous protein that can cause amyloidosis if it accumulates abnormally in organs. In neurological diseases such as Alzheimer's disease (AD) and Parkinson's disease (PD), large amounts of amyloid accumulate and deposit in the nervous system, which is thought to potentially cause degeneration or dysfunction of the brain or other organs.
[0003] A key characteristic of Alzheimer's disease (AD), which affects many elderly people, is the accumulation of beta-amyloid (Aβ) in the brain, which is considered the main cause of dementia worldwide. According to the Alzheimer's Disease International, the number of people with dementia exceeded 50 million in 2020, and is projected to double approximately every 20 years, reaching 82 million in 2030 and 152 million in 2050. Unfortunately, there is no cure for most types of dementia.
[0004] Numerous clinical trials of new Alzheimer's disease treatments have shown that early treatment of the disease should be implemented before the deposition and alteration of beta-amyloid (Aβ) causes irreversible damage to the brain. [Overview of the project] [Problems that the invention aims to solve]
[0005] Conventional amyloidosis treatments have drawbacks such as side effects, chemical synthesis, and insufficient efficacy. There is a need for novel drugs that offer high efficacy in treating amyloidosis to address these issues. [Means for solving the problem]
[0006] In light of this, the object of the present invention is to provide a synthetic peptide containing the amino acid sequence shown in SEQ ID NO: 1.
[0007] In one embodiment of the present invention, the synthetic peptide targets β-amyloid (amyloid β, Aβ).
[0008] In one embodiment of the present invention, the synthetic peptide prevents the formation of β-amyloid aggregation.
[0009] In one embodiment of the present invention, the synthetic peptide prevents the folding and aggregation of total amyloid-beta.
[0010] In one embodiment of the present invention, the total amyloid is β-amyloid (Aβ), tau protein, α-synuclein (α-Syn), islet amyloid polypeptide (IAPP), or transthyretin (TTR).
[0011] In one embodiment of the present invention, the tau protein is recombinant tau P301L protein.
[0012] In one embodiment of the present invention, the TTR is recombinant TTR V122I.
[0013] In one embodiment of the present invention, the TTR is recombinant TTR V30I.
[0014] In one embodiment of the present invention, the synthetic peptide is 1-methyl-4-phenylpyridinium (MPP) + This maintains the cell viability of dopaminergic-like neurons derived from SH-SY5Y that have been treated with this method.
[0015] In one embodiment of the present invention, the synthetic peptide is MPP + and inhibits the formation of amyloid aggregates in dopaminergic-like neurons derived from SH-SY5Y treated with MPP
[0016] In one embodiment of the present invention, the synthetic peptide inhibits the formation of amyloid aggregates in neuron cells derived from SH-SY5Y treated with Aβ
[0017] Another object of the present invention is to provide a pharmaceutical composition comprising the synthetic peptide and a pharmaceutically acceptable carrier
[0018] Another object of the present invention is to provide the use of the synthetic peptide for use in manufacturing a medicament for treating amyloidosis
[0019] In one embodiment of the present invention, the amyloidosis is Parkinson's disease (PD) or Alzheimer's disease (AD)
Effects of the Invention
[0020] In summary, as shown in the following examples, the present invention has the effect of treating amyloidosis (for example, Parkinson's disease and Alzheimer's disease)
Brief Description of the Drawings
[0021] [Figure 1] Shows the affinity of the PAA peptide for tau fibrils [Figure 2] Shows the preventive effect of the PAA peptide on the folding and aggregation of total amyloid β (Aβ) [Figure 3] Shows the preventive effect of the PAA peptide on the folding and aggregation of total amyloid β (Tau) [Figure 4]This study demonstrates the inhibitory effect of PAA peptides on the aggregation of tau protein (P301L). [Figure 5] This study demonstrates the inhibitory effect of PAA peptides on the folding and aggregation of total amyloid-beta (α-Syn). [Figure 6] This study demonstrates the inhibitory effect of PAA peptides on the folding and aggregation of total amyloid-beta (IAPP). [Figure 7] This study demonstrates the inhibitory effect of PAA peptides on the folding and aggregation of total amyloid-beta (TTR V122I). [Figure 8] This study demonstrates the inhibitory effect of PAA peptides on the folding and aggregation of total amyloid-beta (TTR V30I). [Figure 9] This shows the uptake of dopaminergic-like neurons derived from SH-SY5Y treated with 1-methyl-4-phenylpyridinium (MPP)+ into PAA peptide. FITC represents fluorescein isothiocyanate. [Figure 10] This shows the uptake of PAA peptide by Aβ--treated SH-SY5Y-derived neurons. [Figure 11] This study demonstrates the effect of PAA peptides on maintaining cell viability in dopaminergic-like neurons derived from SH-SY5Y cells treated with MPP+. [Figure 12] This study demonstrates the effect of PAA peptides on maintaining cell viability in Aβ-treated SH-SY5Y-derived neuronal cells. [Figure 13] This study demonstrates the inhibitory effect of PAA peptides on the formation of amyloid aggregates in dopaminergic-like neurons derived from SH-SY5Y cells treated with MPP+. [Figure 14] This study demonstrates the inhibitory effect of PAA peptides on the formation of amyloid aggregates in Aβ-treated SH-SY5Y-derived neuronal cells. [Modes for carrying out the invention]
[0022] The following describes embodiments for carrying out the invention, but the embodiments shown below are used to illustrate the present invention and do not limit the scope of the present invention. The scope of the present invention is defined by the claims and can be modified as appropriate by those skilled in the art without departing from the scope of the object of the present invention.
[0023] definition The values described herein are approximate. All experimental data indicate that the values are within a range of ±20%, preferably ±10%, and more preferably ±5%.
[0024] In this specification (especially in the claims), unless otherwise specified, “a,” “the,” and similar terms include both singular and plural forms.
[0025] As used herein, “treating” means alleviating, reducing, ameliorating, relieving, or controlling one or more clinical signs of a disease or disorder, and lowering, stopping, or reversing the progression of the severity of a condition or symptom during treatment.
[0026] The pharmaceuticals of the present invention may be manufactured to be applied to parenterally or orally administered dosage forms by the prior art known to those skilled in the art. The dosage forms include, but are not limited to, injections [e.g., sterile aqueous solution or dispersion], sterile powder, tablets, lozenges, pills, capsules, dispersible powder or granules, solutions, suspensions, emulsions, syrups, elixirs, slurries and similar products.
[0027] The pharmaceutical product of the present invention may be administered via parenteral routes. The parenteral routes are selected from the group consisting of intraperitoneal injection, subcutaneous injection, intraepidermal injection, intradermal injection, intramuscular injection, intravenous injection, and intralesional injection.
[0028] The pharmaceutical product of the present invention may contain a pharmaceutically acceptable carrier widely used in pharmaceutical manufacturing technology. The pharmaceutically acceptable carrier may contain, for example, one or more reagents selected from the group consisting of solvents, emulsifiers, suspending agents, decomposers, binding agents, excipients, stabilizing agents, chelating agents, diluents, gelling agents, preservatives, lubricants, absorption delaying agents, liposomes, and similar substances. A person skilled in the art can select the reagents and their quantities according to the requirements.
[0029] The pharmaceutically acceptable carrier may contain a solvent. The solvent is selected from the group consisting of water, normal saline, phosphate-buffered saline (PBS), sugar solution, alcohol-containing aqueous solution, and combinations thereof.
[0030] The present invention will be described below with reference to examples, but these examples are not intended to limit the present invention. The scope of the present invention is as defined in the claims.
[0031] In this embodiment, the synthetic peptide of the present invention (hereinafter referred to as PAA peptide) contains the amino acid sequence shown in SEQ ID NO: 1.
[0032] In this embodiment, the β-amyloid-targeting PAA peptide is used to treat Parkinson's disease (PD) and Alzheimer's disease (AD).
[0033] Example 1. Production of the synthetic peptide of the present invention In this example, a synthetic peptide (hereinafter referred to as PAA peptide) is synthesized by a conventional solid-phase peptide synthesis method.
[0034] Example 2. Affinity of the PAA peptide of the present invention to tau fibrils In this example, the affinity of PAA peptides to tau fibrils is measured. The experimental procedure is as follows: The binding affinity of PAA peptides is measured by surface plasmon resonance binding assay (SPR binding assay). SPR analysis is performed using CM5 and NTA chips with a BIAcore T200 (Biacore-GE Healthcare, Piscataway, NJ).
[0035] Since a larger surface area is preferable for fixation to the tip, the protein (tau recombinant protein) sample is diluted to a concentration of 20 μg / mL using a 10 mM buffer solution (pH 4.0, 5.5, or 6.0) and spotted onto the tip under conditions of high ligand surface concentration (PAA peptide: 50, 25, 12.5, 6.25, 3.125, and 1.5625 nM) according to the surface treatment process.
[0036] Then, the regeneration method is selected according to regeneration scouting and surface performance testing, and the experiment is conducted. Protein binding is then analyzed using binding analysis and direct binding. Dynamical analysis of the binding test is performed using dynamical analysis and mass transfer. After that, the data is analyzed and the dynamical constants are determined.
[0037] Figure 1 shows the affinity of the PAA peptide to tau fibrils. As can be seen from the SPR affinity analysis results in Figure 1, the affinity of the PAA peptide to tau protein is approximately KD = 7.18 × 10 nM.
[0038] Example 3. Cell-free model for testing the inhibitory effect of PAA peptide on β-amyloid aggregation. In this example, a cell-free model is used to test the inhibitory effect of PAA peptides on β-amyloid aggregation. The experimental procedure is as follows: Each well of a 96-well plate is coated with heparin (50 IU / ml, 50 ml) at 37°C for 30 minutes, and then recombinant amyloid (50 μM) is added. Then, PAA peptides of 0, 3.125, 6.25, 12.5, 25, and 50 μM are cultured in the wells, and 25 nM thioflavin is added. The fluorescence signal is measured using an ELISA reader within a certain time after the reaction.
[0039] Example 4. Effect of PAA peptide on preventing folding and aggregation of total amyloid-beta (β-amyloid (amyloid β, Aβ)). The procedure for this embodiment is as follows: Each well of a 96-well plate is coated with heparin (50 IU / ml, 50 μl) at 37°C for 30 minutes, and then recombinant Aβ peptide (1-42) (50 μM) is added. Then, PAA peptides of 0, 3.125, 6.25, 12.5, 25, and 50 μM are reacted in the wells, and 25 nM thioflavin is added. The fluorescence signal is measured with an ELISA reader within a certain time after reaction. Scale bar = 50 μm. Data are shown as mean ± standard error of the mean (SEM). The results are compared with a 0 μM control group by one-way ANOVA. Statistical significance is set to p < 0.05, *p < 0.05, **p < 0.01, and ***p < 0.001.
[0040] Figure 2 shows the inhibitory effect of PAA peptide on the folding and aggregation of total amyloid-beta (Aβ). As can be seen from Figure 2, PAA peptide can prevent the folding and aggregation of total amyloid-beta (Aβ). The results of the 24-hour fluorescence image (left figure) and the fluorescence quantification results at each time point (right figure) show that it has a dose-dependent inhibitory effect on Aβ aggregation.
[0041] Example 5. Effect of PAA peptide on preventing folding and aggregation of total amyloid-beta (Tau). The procedure for this embodiment is as follows: Each well of a 96-well plate is coated with heparin (50 IU / ml, 50 μl) at 37°C for 30 minutes, and then recombinant tau protein (50 μM) is added. Then, 0, 3.125, 6.25, 12.5, 25, and 50 μM PAA peptides are reacted in the wells, and 25 nM thioflavin is added. The fluorescence signal is measured with an ELISA reader within a certain time after reaction. Scale bar = 50 μm. Data are shown as mean ± standard error of the mean (SEM). The results are compared with a 0 μM control group by one-way ANOVA. Statistical significance is set to p < 0.05, ** p < 0.01, and *** p < 0.001.
[0042] Figure 3 shows the inhibitory effect of PAA peptide on the folding and aggregation of total amyloid-beta (Tau). As can be seen from Figure 3, PAA peptide can prevent the folding and aggregation of amyloid tau (Tau). The results of the 24-hour fluorescence image (left figure) and the fluorescence quantification results at each time point (right figure) show that it has a dose-dependent inhibitory effect on tau aggregation.
[0043] Example 6. Effect of PAA peptide on preventing tau protein (P301L) aggregation The procedure for this embodiment is as follows: Each well of a 96-well plate is coated with heparin (50 IU / ml, 50 μl) at 37°C for 30 minutes, and then recombinant tau P301L protein (50 μM) is added. Then, 0, 3.125, 6.25, 12.5, 25, and 50 μM PAA peptides are reacted in the wells, and 25 nM thioflavin is added. The fluorescence signal is measured using an ELISA reader within a certain time after reaction. Scale bar = 50 μm. Data are shown as mean ± standard error of the mean (SEM). The results are compared with a 0 μM control group by one-way ANOVA. Statistical significance is set to p < 0.05, *p < 0.05, **p < 0.01, and ***p < 0.001.
[0044] Figure 4 shows the inhibitory effect of PAA peptide on tau protein (P301L) aggregation. As can be seen from Figure 4, PAA peptide can prevent the folding and aggregation of amyloid tau (P301L). The 24-hour fluorescence image (left figure) and the fluorescence quantification results at each time point (right figure) demonstrate a dose-dependent inhibitory effect on tau (P301L) aggregation.
[0045] Example 7. Effect of PAA peptide on preventing folding and aggregation of total amyloid-beta (α-Syn). The procedure for this embodiment is as follows: Each well of a 96-well plate is coated with heparin (50 IU / ml, 50 μl) at 37°C for 30 minutes, and then recombinant α-synuclein (α-Syn) PFF (Preformed Fibril) (10 μM) and monomer (50 μM) are added. Then, 0, 3.125, 6.25, 12.5, 25, and 50 μM PAA peptides are reacted in the wells, and 25 nM thioflavin is added. The fluorescence signal is measured using an ELISA reader within a certain time after reaction. Scale bar = 50 μm. Data are shown as mean ± standard error of the mean (SEM). The results are compared with a 0 μM control group by one-way ANOVA. Statistical significance is set to p < 0.05, *p < 0.05, **p < 0.01, and ***p < 0.001.
[0046] Figure 5 shows the inhibitory effect of PAA peptide on the folding and aggregation of total amyloid-beta (α-Syn). As can be seen from Figure 5, PAA peptide can prevent the folding and aggregation of α-synuclein (α-Syn). The results of the 24-hour fluorescence image (left figure) and the fluorescence quantification results at each time point (right figure) show that it has a dose-dependent inhibitory effect on α-Syn aggregation.
[0047] Example 8. Effect of PAA peptide on preventing folding and aggregation of total amyloid-beta (IAPP) The procedure for this example is as follows: Each well of a 96-well plate is coated with heparin (50 IU / ml, 50 μl) at 37°C for 30 minutes, and then recombinant islet amyloid polypeptide (IAPP) peptide (1-37) (50 μM) is added.
[0048] Then, 0, 3.125, 6.25, 12.5, 25, and 50 μM PAA peptides are reacted in the wells, and 25 nM thioflavin is added. The fluorescence signal is measured with an ELISA reader within a certain time after reaction. Scale bar = 50 μm. Data are shown as mean ± standard error of the mean (SEM). One-way ANOVA is performed to compare with a 0 μM control group. Statistical significance is set at p<0.05, *p<0.05, **p<0.01, and ***p<0.001.
[0049] Figure 6 shows the inhibitory effect of PAA peptide on the folding and aggregation of total amyloid-beta (IAPP). As can be seen from Figure 6, PAA peptide can prevent the folding and aggregation of islet amyloid polypeptide (IAPP). The results of the 24-hour fluorescence image (left figure) and the fluorescence quantification results at each time point (right figure) show that it has a dose-dependent inhibitory effect on IAPP aggregation.
[0050] Example 9. Effect of PAA peptide on preventing folding and aggregation of total amyloid-beta (TTR V122I) The procedure for this embodiment is as follows: Each well of a 96-well plate is coated with heparin (50 IU / ml, 50 μl) at 37°C for 30 minutes, and then recombinant transthyretin (TTR) (V122I) (100 μM) is added. Then, 0, 3.125, 6.25, 12.5, 25, and 50 μM PAA peptides are reacted in the wells, and 25 nM thioflavin is added. The fluorescence signal is measured using an ELISA reader within a certain time after reaction. Scale bar = 50 μm. Data are shown as mean ± standard error of the mean (SEM). The results are compared with a 0 μM control group by one-way ANOVA. Statistical significance is p < 0.05, *p < 0.05, **p < 0.01.
[0051] Figure 7 shows the inhibitory effect of PAA peptide on the folding and aggregation of total amyloid-beta (TTR V122I). As can be seen from Figure 7, PAA peptide can prevent the folding and aggregation of transthyretin (Transthyretin V122I, TTR V122I). The results of the 24-hour fluorescence image (left figure) and the fluorescence quantification results at each time point (right figure) show that it has a dose-dependent inhibitory effect on TTR V122I aggregation.
[0052] Example 10. Effect of PAA peptide on preventing folding and aggregation of total amyloid-beta (TTR V30I) The procedure for this embodiment is as follows: Each well of a 96-well plate is coated with heparin (50 IU / ml, 50 μl) at 37°C for 30 minutes, and then recombinant transthyretin (TTR) (V30I) (100 μM) is added. Then, 0, 3.125, 6.25, 12.5, 25, and 50 μM PAA peptides are reacted in the wells, and 25 nM thioflavin is added. The fluorescence signal is measured using an ELISA reader within a certain time after reaction. Scale bar = 50 μm. Data are shown as mean ± standard error of the mean (SEM). The results are compared with a 0 μM control group by one-way ANOVA. Statistical significance is p < 0.05, *p < 0.05, **p < 0.01.
[0053] Figure 8 shows the inhibitory effect of PAA peptide on the folding and aggregation of total amyloid-beta (TTR V30I). As can be seen from Figure 8, PAA peptide can prevent the folding and aggregation of transthyretin V30I (TTR V30I). The results of the 24-hour fluorescence image (left figure) and the fluorescence quantification results at each time point (right figure) show that it has a dose-dependent inhibitory effect on TTR V30I aggregation.
[0054] Example 11. MPP for PAA peptide + Uptake of dopaminergic-like neurons derived from SH-SY5Y processed with The procedure for this embodiment is as follows: 1-methyl-4-phenylpyridinium (MPP) + SH-SY5Y-derived dopaminergic-like neurons treated with [specific agent] were then treated with fluorescein isothiocyanate (FITC)-conjugated PAA peptide (0, 1, 2.5, 5, 10 μg / ml) for 4 hours, and the fluorescence signal was measured by microscopy (upper figure) and flow cytometry (lower figure).
[0055] Figure 9 shows the relationship between 1-methyl-4-phenylpyridinium (MPP) and PAA peptide. + This shows the uptake of dopaminergic-like neurons derived from SH-SY5Y treated with [method]. As can be seen from the fluorescence image (top) and flow cytometry (bottom) results in Figure 9, as the amount of PAA peptide increases, MPP for PAA peptide increases. + The uptake rate of dopaminergic-like neurons derived from SH-SY5Y treated with this agent also increases.
[0056] Example 12. Uptake of PAA peptide by Aβ--treated SH-SY5Y-derived neurons The procedure for this embodiment is as follows: Aβ-treated SH-SY5Y-derived neurons were treated with FITC-bound PAA peptide (0, 1, 2.5, 5, 10 μg / ml) for 4 hours, and then the fluorescence signal was measured by microscopy (upper figure) and flow cytometry (lower figure).
[0057] Figure 10 shows the uptake of Aβ-treated SH-SY5Y-derived neuron cells against the PAA peptide. As can be seen from the results of the fluorescence image (top) and flow cytometry (bottom) in Figure 10, as the amount of the PAA peptide increases, the uptake amount of the Aβ-treated SH-SY5Y-derived neuron cells against the PAA peptide also increases.
[0058] Example 13. Maintenance effect of cell viability of MPP + -treated SH-SY5Y-derived dopaminergic-like neurons by the PAA peptide The procedure of this example is as follows. After treating MPP + -treated SH-SY5Y-derived dopaminergic-like neurons with the PAA peptide (0, 1, 2.5, 5, 10 μg / ml) for 96 hours, flow cytometry is used to stain with propidium iodide (PI) to measure the cell viability.
[0059] Figure 11 shows the maintenance effect of cell viability of MPP + -treated SH-SY5Y-derived dopaminergic-like neurons by the PAA peptide. As can be seen from the results of the flow cytometry in Figure 11, the PAA peptide can significantly reduce the cell death of MPP + -treated SH-SY5Y-derived dopaminergic-like neurons.
[0060] Example 14. Maintenance effect of cell viability of Aβ-treated SH-SY5Y-derived neuron cells by the PAA peptide The procedure of this example is as follows. After treating Aβ-treated SH-SY5Y-derived neuron cells with the PAA peptide (0, 1, 2.5, 5, 10 μg / ml) for 96 hours, flow cytometry is used to stain with PI to measure the cell viability.
[0061] Figure 12 shows the effect of PAA peptide on maintaining cell viability in Aβ--treated SH-SY5Y-derived neurons. As can be seen from the flow cytometry analysis results in Figure 12, PAA peptide can significantly reduce cell death in Aβ-- treated SH-SY5Y-derived neurons.
[0062] Example 15. MPP using PAA peptide + Inhibitory effect of amyloid aggregate formation in dopaminergic-like neurons derived from SH-SY5Y treated with [method name]. The procedure for this embodiment is as follows: MPP + Dopaminergic-like neurons derived from SH-SY5Y, treated with [specified method], were then treated with PAA peptide (2.5 μg / ml) for 96 hours. Immunofluorescence staining was then used to measure the presence of Aβ, Tau, and α-Syn. Aggregation was then observed using a confocal microscope.
[0063] Figure 13 shows MPP mediated by PAA peptide. + It shows an inhibitory effect on the formation of amyloid aggregates in dopaminergic-like neurons derived from SH-SY5Y treated with it. As can be seen from the fluorescence microscopy images in Figure 13, the PAA peptide inhibits MPP + This method significantly reduces the aggregation of Aβ, Tau, and α-Syn in dopaminergic-like neuronal cells derived from SH-SY5Y that have been treated with this method.
[0064] Example 16. Inhibitory effect of PAA peptide on the formation of amyloid aggregates in Aβ-treated SH-SY5Y-derived neuronal cells. The procedure for this example is as follows: Aβ-treated SH-SY5Y-derived neurons are treated with PAA peptide (2.5 μg / ml) for 96 hours, and then Aβ, Tau, and α-Syn detection are measured by immunofluorescence staining. Aggregation is then observed using a confocal microscope.
[0065] Figure 14 shows the inhibitory effect of PAA peptide on the formation of amyloid aggregates in Aβ-treated SH-SY5Y-derived neurons. As can be seen from the fluorescence microscopy images in Figure 14, PAA peptide can significantly reduce the aggregation of Aβ, Tau, and α-Syn in Aβ-treated SH-SY5Y-derived neurons.
[0066] As described above, the present invention has the effect of treating amyloidosis (for example, Parkinson's disease and Alzheimer's disease), as shown in the results of the above examples.
[0067] The present invention is not limited to the above. Equivalent modifications made without departing from the scope of the present invention are all included within the scope of the claims of the present invention.
Claims
1. The amino acid sequence includes the sequence shown in Sequence ID No. 1, Synthetic peptide.
2. Targeting β-amyloid (amyloid β, Aβ), The synthetic peptide according to claim 1.
3. To prevent the formation of β-amyloid aggregates, The synthetic peptide according to claim 2.
4. To prevent the folding and aggregation of all amyloid-beta, The synthetic peptide according to claim 3.
5. The aforementioned amyloid is β-amyloid (Aβ), tau protein, α-synuclein (α-Syn), islet amyloid polypeptide (IAPP), or transthyretin (TTR). The synthetic peptide according to claim 4.
6. The aforementioned tau protein is recombinant tau P301L protein. The synthetic peptide according to claim 5.
7. The aforementioned TTR is recombinant TTR V122I. The synthetic peptide according to claim 5.
8. The aforementioned TTR is recombinant TTR V30I. The synthetic peptide according to claim 5.
9. 1-Methyl-4-phenylpyridinium (MPP) + The synthetic peptide according to claim 1, which maintains the cell viability of dopaminergic-like neurons derived from SH-SY5Y treated with the peptide.
10. MPP + It inhibits the formation of amyloid aggregates in dopaminergic-like neurons derived from SH-SY5Y treated with this method. The synthetic peptide according to claim 1.
11. The synthetic peptide according to claim 1, which inhibits the formation of amyloid aggregates in Aβ-treated SH-SY5Y-derived neuronal cells.
12. A synthetic peptide according to any one of claims 1 to 11 and a pharmaceutically acceptable carrier, Pharmaceutical composition.
13. Used to manufacture drugs that treat amyloidosis. Use of the synthetic peptide according to any one of claims 1 to 11.
14. The aforementioned amyloidosis is Parkinson's disease (PD) or Alzheimer's disease (AD). Use of the synthetic peptide according to claim 13.