Mapping of possible binding sequences of two beta-sheet breaker peptides on beta amyloid peptide of Alzheimer's disease

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Abstract

Aggregation of amyloid peptide (Aβ) has been identified as a major feature of the pathogenesis of Alzheimer's disease. Increased risk for disease is associated with increased formation of polymerized Aβ. Inhibition of formation of toxic (aggregated) form of Aβ is one of the therapeutic possibilities. Beta sheet breaker peptides (BSBs) fulfill the requirements of an effective inhibitor. After having attached to the Aβ molecules, BSBs can prevent aggregation of Aβ to polymeric forms (aggregates). In the present study, we performed molecular modelling of complex formation between Aβ and two BSB peptides. Our aim was to find proper binding sequences for the BSB peptides on Aβ and characterize them. A dimeric model of Aβ was also used to study the interaction of BSBs with the aggregated forms of Aβ and find the sequences responsible for the polymerization process. A fast and efficient computational method: molecular docking was used for the afore-mentioned purposes.

Original languageEnglish
Pages (from-to)1587-1593
Number of pages7
JournalBioorganic and Medicinal Chemistry
Volume10
Issue number5
DOIs
Publication statusPublished - 2002

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Amyloid beta-Peptides
Alzheimer Disease
Peptides
Agglomeration
Molecular modeling
Poisons
Computational methods
Amyloid
Polymerization
Molecules
beta-Strand Protein Conformation
Therapeutics

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science

Cite this

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abstract = "Aggregation of amyloid peptide (Aβ) has been identified as a major feature of the pathogenesis of Alzheimer's disease. Increased risk for disease is associated with increased formation of polymerized Aβ. Inhibition of formation of toxic (aggregated) form of Aβ is one of the therapeutic possibilities. Beta sheet breaker peptides (BSBs) fulfill the requirements of an effective inhibitor. After having attached to the Aβ molecules, BSBs can prevent aggregation of Aβ to polymeric forms (aggregates). In the present study, we performed molecular modelling of complex formation between Aβ and two BSB peptides. Our aim was to find proper binding sequences for the BSB peptides on Aβ and characterize them. A dimeric model of Aβ was also used to study the interaction of BSBs with the aggregated forms of Aβ and find the sequences responsible for the polymerization process. A fast and efficient computational method: molecular docking was used for the afore-mentioned purposes.",
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AU - Hetényi, C.

AU - Körtvélyesi, T.

AU - Penke, B.

PY - 2002

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AB - Aggregation of amyloid peptide (Aβ) has been identified as a major feature of the pathogenesis of Alzheimer's disease. Increased risk for disease is associated with increased formation of polymerized Aβ. Inhibition of formation of toxic (aggregated) form of Aβ is one of the therapeutic possibilities. Beta sheet breaker peptides (BSBs) fulfill the requirements of an effective inhibitor. After having attached to the Aβ molecules, BSBs can prevent aggregation of Aβ to polymeric forms (aggregates). In the present study, we performed molecular modelling of complex formation between Aβ and two BSB peptides. Our aim was to find proper binding sequences for the BSB peptides on Aβ and characterize them. A dimeric model of Aβ was also used to study the interaction of BSBs with the aggregated forms of Aβ and find the sequences responsible for the polymerization process. A fast and efficient computational method: molecular docking was used for the afore-mentioned purposes.

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