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Design of Distamicin Analogues to Probe the Physical Origin of the Antiparallel Side by Side Oligopeptide Binding Motif in DNA Minor Groove Recognition
- Source :
- Biochemical and Biophysical Research Communications. 220:213-218
- Publication Year :
- 1996
- Publisher :
- Elsevier BV, 1996.
-
Abstract
- Oligopeptides distamycin and its analogues can bind cooperatively to the minor groove of certain DNA sequences in a closely compacted antiparallel side by side motif, where the positively charged ends are located in the carboxyl termini of such peptidic structures. In order to dissect its physical underpinning, the role of charge in maintaining the integrity of this novel motif is explored by using three judiciously designed distamycin analogues possessing either no charge or with charge ends located in the amino termini. Preliminary experiments by CD and ethidium fluorescence displacement suggested that the charge plays an role in influencing the degree of binding cooperativity as well as binding strength, although qualitatively the dimeric binding remains cooperative.
- Subjects :
- genetic structures
Stereochemistry
Molecular Sequence Data
Biophysics
Cooperativity
In Vitro Techniques
Biology
Antiparallel (biochemistry)
Biochemistry
chemistry.chemical_compound
Poly dA-dT
Molecular Biology
Oligopeptide
Binding Sites
Base Sequence
Molecular Structure
Circular Dichroism
Distamycins
Distamycin
DNA
Cell Biology
chemistry
Drug Design
Molecular Probes
Oligopeptides
Oligopeptide binding
Minor groove
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 220
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....a742a4391975caccff1f7dd1c8fa4089