Rational design and synthesis of a double-stranded DNA-binder library
Language English Country United States Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
16498625
DOI
10.1002/bip.20487
Knihovny.cz E-resources
- MeSH
- Aminacrine chemistry MeSH
- Computer-Aided Design MeSH
- DNA-Binding Proteins chemistry metabolism MeSH
- DNA chemical synthesis chemistry metabolism MeSH
- Fluorescent Dyes chemistry MeSH
- Gene Library * MeSH
- Intercalating Agents chemistry MeSH
- Humans MeSH
- Models, Molecular MeSH
- Peptide Fragments metabolism MeSH
- Prions metabolism MeSH
- Cattle MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- Combinatorial Chemistry Techniques MeSH
- Thymus Gland chemistry MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Aminacrine MeSH
- DNA-Binding Proteins MeSH
- DNA MeSH
- Fluorescent Dyes MeSH
- Intercalating Agents MeSH
- Peptide Fragments MeSH
- prion protein (106-126) MeSH Browser
- Prions MeSH
Described is a computer-assisted rational design of a DNA-bis-intercalator peptide library. The peptide library of 250 members was prepared and the most powerful binder identified. A value of the binding constant is almost two orders of magnitude higher than that of starting building block-9-aminoacridine. The binder affinity found toward calf thymus DNA is 30-fold of that of human prion peptide 106-126.
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