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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Amyloid Fibrils03:03

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Design Example: Aggregate Gradation01:24

Design Example: Aggregate Gradation

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The right type and quality of aggregates are crucial for concrete as they significantly influence its properties, mix proportions, and cost-effectiveness. If different sources are available for sand, the commonly used fine aggregate in concrete, the selection of sand is primarily based on its gradation.
The grading, or particle-size distribution, of sand is determined using sieve analysis, with standard sizes ranging from 150 μm to 10 mm (ASTM No. 100 sieve to 3⁄8 in. sieve). Sand is...
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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Peptide Bonds02:43

Peptide Bonds

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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Structure-Activity Relationships and Drug Design01:28

Structure-Activity Relationships and Drug Design

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Drug design is a dynamic field that involves discovering and developing new medications based on specific biological targets. This process heavily relies on structure-activity relationships (SAR) and quantitative structure-activity relationships (QSAR) to guide the design and optimization of efficient drugs.
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Updated: Jan 27, 2026

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
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Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

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Structure-Based Peptide Inhibitor Design of Amyloid-β Aggregation.

Jinxia Lu1, Qin Cao2, Chuchu Wang3,4

  • 1Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders (Ministry of Education), Bio-X Institutes, Shanghai Jiao Tong University, Shanghai, China.

Frontiers in Molecular Neuroscience
|March 20, 2019
PubMed
Summary
This summary is machine-generated.

Researchers designed potent peptide inhibitors to block amyloid-beta (Aβ) aggregation, a key factor in neurodegenerative diseases. This structure-based approach with chemical modification offers a promising therapeutic strategy for amyloid-related conditions.

Keywords:
Alzheimer’s diseaseAβ fibrilneurodegenerative diseasesprotein misfoldingstructure-based inhibitor design

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Drug Discovery

Background:

  • Amyloid fibril formation is implicated in human neurodegenerative diseases.
  • Developing selective and potent amyloid inhibitors is a significant therapeutic challenge.

Purpose of the Study:

  • To design novel peptide inhibitors targeting amyloid-beta (Aβ) aggregation.
  • To improve inhibitor potency and selectivity through structure-based design and chemical modification.

Main Methods:

  • Utilized RosettaDesign based on Aβ fibril structures to design peptide inhibitors.
  • Employed a chemical scaffold to constrain peptides into a β-strand conformation.
  • Assessed inhibitor potency against Aβ aggregation and toxicity.

Main Results:

  • Designed peptide inhibitors demonstrated improved potency against Aβ aggregation and toxicity.
  • Chemical constraint into β-strand conformation significantly enhanced inhibitor efficacy.
  • Targeting different Aβ segments allowed for selective recognition of various Aβ species.

Conclusions:

  • A combined structure-based rational design and chemical modification approach effectively yields potent amyloid inhibitors.
  • This strategy holds potential for developing therapeutics for diverse amyloid-related diseases.