Cyclic Amyloid Inhibitory Peptides for BBB-Penetrant α-Synuclein Binding

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Solution Overview

Problem

Current inhibitors for amyloid self-assembly, particularly for α-synuclein (αSyn) and islet amyloid polypeptide (IAPP), face challenges such as high conformational flexibility, low blood-brain-barrier permeability, high production costs, potential immunogenicity, and lack of specificity and affinity, making them unsuitable for clinical use in treating synucleinopathies like Parkinson's disease.

Innovation Solution

Development of cyclic peptides with specific amino acid sequences that bind to α-synuclein and IAPP with nanomolar affinity, inhibiting amyloid self-assembly and cross-seeding interactions, and are capable of crossing the blood-brain barrier.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If linear peptides are used to inhibit amyloid self-assembly, then they can bind to amyloidogenic polypeptides, but they have low blood-brain-barrier permeability and cannot cross the BBB

Engineering Contradiction:
Improveamyloid inhibition efficacyVSAvoidblood-brain-barrier permeability
Core Design Contradiction:
ReliabilityVSEase of operation

Solution Approach 1:

The patent applies parameter changes by converting linear peptides into cyclic structures through disulfide bonds between cysteine residues. This structural transformation changes the conformational flexibility parameter, creating a more rigid and stable cyclic peptide architecture that maintains amyloid binding capability while improving blood-brain-barrier permeability for CNS delivery

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The invention employs spheroidality by introducing cyclic structures with curved three-dimensional conformations. The cyclic peptides adopt defined spatial arrangements that differ from linear extensions, creating a more compact and potentially BBB-penetrable structure while maintaining the ability to bind amyloidogenic polypeptides

Inventive Principle:
Principle #14Spheroidality (Curvature)

2Reliability

If antibodies are used to inhibit amyloid self-assembly, then they have high affinity and specificity, but they have high production costs and potential immunogenicity

Engineering Contradiction:
Improvebinding affinity and specificityVSAvoidproduction cost and immunogenicity
Core Design Contradiction:
ReliabilityVSEase of manufacture

Solution Approach 1:

The patent applies extraction by isolating and utilizing only the essential antigen-binding fragments (peptides) from antibody structures. By extracting the functional binding domain and removing the problematic Fc region and other antibody components, the invention achieves high affinity binding with reduced production costs and immunogenicity

Inventive Principle:
Principle #2Taking out (Extraction)

Solution Approach 2:

The invention employs cheap short-living objects by using synthetic peptides instead of full-length antibodies. These peptides are cheaper to produce, can be synthesized readily, and while potentially having shorter half-lives, provide cost-effective therapeutic or diagnostic solutions for amyloid-related diseases

Inventive Principle:
Principle #27Cheap short-living objects (Disposable)

3Ease of manufacture

If small molecules are used to inhibit amyloid self-assembly, then they have low production costs and good permeability, but they lack high affinity and specificity and cannot block interactions involving large interfaces

Engineering Contradiction:
Improveproduction cost and permeabilityVSAvoidbinding affinity and specificity
Core Design Contradiction:
Ease of manufactureVSReliability

Solution Approach 1:

The patent applies composite materials by creating hybrid structures that combine the advantages of peptides and small molecules. The cyclic peptides incorporate rigid aromatic residues (phenylalanine, tryptophan) and charged residues that provide both the affinity and specificity of large molecules and the permeability characteristics of smaller compounds, effectively blocking large interface interactions

Inventive Principle:
Principle #40Composite materials

Applied Scientific Principles

This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.

Function Achieved in This Case

The peptides effectively suppress both self-seeded and cross-seeded amyloid self-assembly of α-synuclein, offering therapeutic and diagnostic potential for synucleinopathies by binding to key amyloid polypeptides with high affinity, thus providing a treatment and diagnostic tool for diseases like Parkinson's disease.

Implementation Method 1

Amyloid self-assembly is linked to devastating cell-degenerative diseases including Alzheimer's disease (AD), type 2 diabetes (T2D), Parkinson's disease (PD) and dementia with Lewy bodies

Methodology Applied
Scientific EffectAmyloid self-assembly: Self-Assembly

Data Source

PatentEP4686725A1Amyloid inhibitory peptides
Publication Date: 2026.02.04 TECHNISCHE UNIVERSITAT MUNCHEN
  • EP4686725A1 patent drawingFigure 1a~1c
  • EP4686725A1 patent drawingFigure 2a~2c
  • EP4686725A1 patent drawingFigure 2d~2f

AI summary

The present invention relates to peptides, in particular of amyloid inhibitory peptides, and to pharmaceutical compositions comprising such peptides, for use in methods of treating or preventing or delaying the onset of synucleinopathies, in particular of Parkinson's disease (PD) or dementia with Lewy bodies, and their comorbidities, in particular PD/type 2 diabetes (T2D) and PD/Alzheimer's disease (AD). Furthermore, the present invention relates to such peptides, in particular such amyloid inhibitory peptides, for use in methods of diagnosing such synucleinopathies and related comorbidities. Furthermore, the present invention also relates to a kit for the in-vitro or in-vivo detection and, optionally, quantification of amyloidogenic polypeptides, amyloid fibrils or amyloid aggregates, and/or for the diagnosis of synucleinopathies and related comorbidities, in particular PD/type 2 diabetes (T2D) and PD/Alzheimer's disease (AD), in a patient.