Structural Studies of Specific Intermolecular Interactions and Self-Aggregation of Biomolecules and Their Application to Drug Design

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概要

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• Information on the structural basis of intermolecular recognition or self-aggregation of biomolecules at the atomic level is important to understand biological functions and to develop devices for treating disorders caused by abnormal functions. Thus structural analysis of specific intermolecular or intramolecular interactions of biomolecules has been performed using various physicochemical approaches. Herein, the following three subjects are reviewed: (1) structural analyses of mRNA cap structure recognition by eukaryotic initiation factor 4E and its functional regulation by endogenous 4E-binding protein; (2) structural studies of self-aggregation mechanism of microtubule-binding domain in tau protein and aggregation inhibitor; and (3) molecular design of cathepsin B-specific inhibitor.

• 公益社団法人　日本薬学会の論文

著者

• Ishida Toshimasa

  Osaka Univ. Of Pharmaceutical Sciences

関連論文

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• Comparison of Conformations of Tetrapeptide Diastereomers Containing α-Phenyl-α-(2-pyridyl)glycine
• Crystallization and Preliminary X-Ray Diffraction Study of Recombinant Human Eukaryotic Initiation Factor-4E
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• Crystal Structure of Hybrid Dipeptide, (2-Carboxyethyl)-cytosine-1-yl-L-threonine Monohydrate
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• Conformation and Sodium Coordinate Forms of an Endothelin Inhibitor BQ123・Na, Cyclo(-D-Trp-D-Asp^~-Pro-D-Val-Leu-)・Na^+, in the Crystal
• Polymorphism and C-H…O Interaction of Wortmannin, a Phosphatidylinositol 3-Kinase Inhibitor
• Crystal Structure of 3, 4-Dihydroxy-6-fluoro-DL-phenylalanine Monohydrate Used as a Positron Emission Tomography Imaging Ligand
• Interaction Modes between N7-Quarternized Guanine and Cytosine-Containing Dipeptides
• Crystal Structure of Hybrid Dipeptide, Uracil-1-yl-(2-carboxyethyl)-glycine
• Crystal Structure of Cytosine and Alanine Hybrid Dipeptide, Cytosine-1-yl-(2-carboxyethyl)-L-alanine
• Spectroscopic Investigation on the Interaction of NCA0424,a Potent Antitumor Indoloquinoxaline Derivative, with DNA
• Thermodynamic Effect of Commplementary Hydrogen Bond Base Pairing on Aromatic stacking Interaction in the Guanine-X-Trp Complex (X=Adenine, Guanine, Cytosine, Thymine)
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• Opioid Peptide-Like Activities of Fulicin, Fulicin Gene-Related Peptides, and Their Synthetic Analogs
• Domain-dependent Interaction of Eukaryotic Initiation Factor eIF4A for Binding to Middle and C-terminal Domains of eIF4G
• Role of Each Repeat Peptide in Aggregation of Tau Microtubule-binding Domain
• Marked Difference Between Self-aggregations of First and Fourth Repeat Peptides on Tau Microtubule-binding Domain in Acidic Solution
• Study of Self-Aggregation Mechanism of Microtubule-Binding Domain of Tau Protein
• Effect of N-Terminal Region of eIF4E and Ser65-Phosphorylation of 4E-BP1 on Interaction between eIF4E and 4E-BP1 Fragment Peptide
• N-terminal Secondary Structures of Second and Third Repeat Fragments Responsible for Self-assembly of Tau Microtubule-binding Domain
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• Solvent-dependent Conformational Change of Third Repeat Fragment of Microtubule-binding Domain Responsible for Filament Formation of Tau Protein
• Conformational Analysis of Four Repeat Fragments in Tau Microtuble Binding Domain
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• Binding Mode of CA074, a Specific Irreversible Inhibitor, to Bovine Cathepsin B as Determined by X-Ray Crystal Analysis of the Complex
• Structural Studies of C-Amidated Amino Acids and Peptides : Crystal Structures of Z-Gly-Phe-NH_2,Tyr-Lys-NH_2,and Asp-Phe-NH_2
• Solvent-Dependent Conformation of the Third Repeats Fragment in the Microtubule-Binding Domain of Tau Protein, Analyzed by ^1H-NMR Spectroscopy and Molecular Modeling Calculation
• Aggregation Analysis of the Microtubule Binding Domain in Tau Protein by Spectroscopic Methods
• Inhibitory Behavior of Cyanidine and Methylene Blue for Filament Formation of Tau Microtubule-binding Domain
• Structural Studies of [2',6'-Dimethyl-L-tyrosine^1]Endomorphin-2 Analogues Containing Proline Mimics
• Side Chain-Dependent Binding of Antitumor Indoloquinoxaline Derivatives to DNA:Comparative Spectroscopic and Viscometric Measurements
• Importance of Tyrosine Residue for Filament Formation of Tau Microtubule-binding Domain
• Structural Scaffold of 18-Crown-6 Tetracarboxylic Acid for Optical Resolution of Chiral Amino Acid : X-Ray Crystal Analyses of Complexes of D- and L-Isomers of Serine and Glutamic Acid
• Conformational Study of Repeat Fragments in Microtuble Binding Domain of Tau Protein
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• Molecular Conformation of Aureobasidin A, a Potent Antifungal Cyclic Depsipeptide : X-Ray Structure Analysis
• Importance of Tyr310 residue in the third repeat of microtubule binding domain for filament formation of tau protein
• Unique Coordination Mode of Potassium Ions to Glycyrrhizin : X-ray Crystal Structure of Glycyrrhizin Dipotassium Salt
• Structural Studies of Specific Intermolecular Interactions and Self-Aggregation of Biomolecules and Their Application to Drug Design
• CH-π Interaction between I308 and Y310 Residues is Required for Self Assembly of Full Length Tau
• Structural Studies on C-Amidated Amino Acids and Peptides : Function of Amide Group in Molecular Association in Crystal Structures of Val-Gly-NH_2, Ser-Phe-NH_2, Gly-Tyr-NH_2 and Pro-Tyr-NH_2 Hydrochloride Salts
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• The crystal and molecular structure of N-(thioacetyl)tryptamine. A radioprotective indole compound.

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