A beta aggregation inhibitor

Abstract

The invention discloses an A beta aggregation inhibitor. The aggregation inhibitor is characterized in that: the amino acid sequence of the aggregation inhibitor is amino terminal-IYVLIY-carboxyl terminal. The peptide sequence is designed based on a quantitative structure function relational model of peptide and is obtained through technical detection of microscope scan. The aggregation inhibitor has a good effect of inhibiting the aggregation of the toxic body, namely A beta capable of causing Alzheimer's disease and can be further developed into a medicament for treating the Alzheimer's disease.

Description

technical field [0001] The invention relates to an Aβ aggregation inhibitor, in particular to an anti-Alzheimer's toxicant Aβ inhibitor. Background technique [0002] Alzheimer's disease (AD) is the most common dementia in the elderly. At present, at least 35 million people worldwide suffer from this disease, and the annual fatality rate is rising. The total annual global cost is estimated to reach 200 billion US dollars. Studies have shown that Aβ (Amyloid β-peptide) oligomers are significant toxicants in AD patients, so inhibiting the generation of Aβ oligomers is the most effective strategy to prevent AD. However, there is currently no effective method for the design of AD inhibitors, mainly facing three serious challenges: 1. Lack of effective high-throughput screening methods: experimental screening methods need to synthesize and purify Aβ, which is undoubtedly a challenge for the screening of a large number of compounds Time-consuming, expensive and impractical. 2. ...

AI Technical Summary

Problems solved by technology

However, there is currently no effective method for the design of AD inhibitors, mainly facing three serious challenges: 1. Lack of effective high-throughput screening methods: experimental screening methods need to synthesize and purify Aβ, which is undoubtedly a challenge for the screening of a large number of compounds Time-consuming, expensive and impractical

2. Lack of high-resolution structures of Aβ oligomers: Aβ oligomers are in a metastable state, so it is difficult to obtain their structures using X-ray diffraction and NMR techniques, making rational drug design based on structures difficult to achieve

3. Lack of understanding of the mechanism of Aβ self-assembly: including which part of the peptide plays a key role in the process of amyloid fibril generation; what are the pathways and intermediates related to seed and fiber generation; whether Aβ has affinity to specific receptors body; how Aβ generates the toxic body and what is the mechanism of toxicity

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