Abstract
Amyloid fibril formation of amyloid beta peptide 1-40 (Aβ 1-40) was reported to be retarded in the presence of 150mM phosphate buffer at pH 7 [Monji, Ustumi, Ueda, Imoto, Yoshida, Hashioka, Tashiro and Tashiro, J. Neurochemistry, 77, 1425-1432 (2007)]. In order to elucidate the reason why phosphate ion retards the amyloid fibril formation, we examined the preferential binding sites of phosphate ion to Aβ 1-40 using chemical shift perturbation analysis of heteronuclear NMR. In titration analysis of 15N-labeled Aβ1-40 in the presence of 150 mM phosphate ion or 150 mM chloride ion, we identified the residues affected by these ions in Aβ 1-40. As a result, we found the tendency that phosphate ion preferentially bound to some residues located on the C-terminus region where the region was reported to be the potential β-strand region in Aβ1-40. Therefore, we suggested that phosphate ions interacted with the potential β-strand region in Aβ1-40 to be hard to form β-sheet in Aβ 1-40, resulting in retardation of the amyloid fibril formation.
Keywords: Alzheimer's disease, amyloid beta peptide 1-40, chemical shift perturbation analysis, heteronuclear NMR, phosphate ion
Protein & Peptide Letters
Title: Evidence for the Binding of Phosphate Ion to the C-Terminus Region in Aβ1-40 Using Heteronuclear NMR Analyses
Volume: 17 Issue: 2
Author(s): Makiko Nagata-Uchiyama, Yoshito Abe, Akira Monji, Shigenobu Kanba and Tadashi Ueda
Affiliation:
Keywords: Alzheimer's disease, amyloid beta peptide 1-40, chemical shift perturbation analysis, heteronuclear NMR, phosphate ion
Abstract: Amyloid fibril formation of amyloid beta peptide 1-40 (Aβ 1-40) was reported to be retarded in the presence of 150mM phosphate buffer at pH 7 [Monji, Ustumi, Ueda, Imoto, Yoshida, Hashioka, Tashiro and Tashiro, J. Neurochemistry, 77, 1425-1432 (2007)]. In order to elucidate the reason why phosphate ion retards the amyloid fibril formation, we examined the preferential binding sites of phosphate ion to Aβ 1-40 using chemical shift perturbation analysis of heteronuclear NMR. In titration analysis of 15N-labeled Aβ1-40 in the presence of 150 mM phosphate ion or 150 mM chloride ion, we identified the residues affected by these ions in Aβ 1-40. As a result, we found the tendency that phosphate ion preferentially bound to some residues located on the C-terminus region where the region was reported to be the potential β-strand region in Aβ1-40. Therefore, we suggested that phosphate ions interacted with the potential β-strand region in Aβ1-40 to be hard to form β-sheet in Aβ 1-40, resulting in retardation of the amyloid fibril formation.
Export Options
About this article
Cite this article as:
Nagata-Uchiyama Makiko, Abe Yoshito, Monji Akira, Kanba Shigenobu and Ueda Tadashi, Evidence for the Binding of Phosphate Ion to the C-Terminus Region in Aβ1-40 Using Heteronuclear NMR Analyses, Protein & Peptide Letters 2010; 17 (2) . https://dx.doi.org/10.2174/092986610790226058
DOI https://dx.doi.org/10.2174/092986610790226058 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers
Related Articles
-
Meet Our Regional Editor
Current Bioinformatics Revisiting the Medical Management of Parkinson’s Disease: Levodopa versus Dopamine Agonist
Current Neuropharmacology Ligand Based Validated Comparative Chemometric Modeling and Pharmacophore Mapping of Aurone Derivatives as Antimalarial Agents
Current Computer-Aided Drug Design Age-Associated Changes in Immune Function: Impact of Vitamin E Intervention and the Underlying Mechanisms
Endocrine, Metabolic & Immune Disorders - Drug Targets Development of New Staining Technology “Eastern Blotting” Using Monoclonal Antibody
Current Drug Discovery Technologies PPARγ and Its Ligands: Potential Antitumor Agents in the Digestive System
Current Stem Cell Research & Therapy Study of Protein Amyloid-Like Aggregates by Solid-State Circular Dichroism Spectroscopy
Current Protein & Peptide Science Estrogen Regulation of Adipose Tissue Functions: Involvement of Estrogen Receptor Isoforms
Infectious Disorders - Drug Targets Unusual Food Allergy: AlioideaAllergic Reactions Overview
Recent Patents on Inflammation & Allergy Drug Discovery Protein-Protein Interactions in Membranes
Protein & Peptide Letters Anticancer Properties of Flavonoids: Roles in Various Stages of Carcinogenesis
Cardiovascular & Hematological Agents in Medicinal Chemistry Epilepsy, Comorbidities and Treatments
Current Pharmaceutical Design Would Some Herbal Teas Play a Medicating Role for Certain Diseases?
Current Nutrition & Food Science Exploring Multiple Sclerosis (MS) and Amyotrophic Lateral Scler osis (ALS) as Neurodegenerative Diseases and their Treatments: A Review Study
Current Topics in Medicinal Chemistry Methods and Applications of Structure Based Pharmacophores in Drug Discovery
Current Topics in Medicinal Chemistry Neurovascular Mechanisms of Hypertension in Pregnancy
Current Neurovascular Research Biochemical Markers of Bone Turnover and their Role in Osteoporosis Diagnosis: A Narrative Review
Recent Patents on Endocrine, Metabolic & Immune Drug Discovery CD38 as a Regulator of Cellular NAD: A Novel Potential Pharmacological Target for Metabolic Conditions
Current Pharmaceutical Design The Relationship Between Lithium and Cancer Proliferation: A Case-Based Review of the Literature
Current Drug Metabolism Synthesis of Mannich Bases by Two Different Methods and Evaluation of their Acetylcholine Esterase and Carbonic Anhydrase Inhibitory Activities
Letters in Drug Design & Discovery