Abstract
Structure-activity relationship (SAR) analysis was applied for studies of docking of colored ligands to library of artificial receptors formed by self-assembly of N-lipidated amino acids immobilised on the cellulose support. The studies show that the binding depends mainly on the structure of amino acid fragment but influence of N-lipidic fragment is less important.
Copyright © 2010 Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acids / chemistry
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Amino Acids / metabolism
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Binding Sites
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Biocompatible Materials / chemistry*
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Biocompatible Materials / metabolism
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Biosensing Techniques / methods*
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Cellulose / chemistry
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Coloring Agents / chemistry
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Coloring Agents / metabolism
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Combinatorial Chemistry Techniques / methods*
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Enzymes, Immobilized / chemistry
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Enzymes, Immobilized / metabolism
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Ligands
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Lipids / chemistry
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Nitrogen / chemistry
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Nitrogen / metabolism
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Proteins / chemistry*
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Proteins / metabolism
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Receptors, Peptide / chemistry*
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Receptors, Peptide / metabolism
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Structure-Activity Relationship
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Triazines / chemistry
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Triazines / metabolism
Substances
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Amino Acids
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Biocompatible Materials
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Coloring Agents
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Enzymes, Immobilized
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Ligands
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Lipids
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Proteins
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Receptors, Peptide
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Triazines
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Cellulose
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Nitrogen