|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
1997-1-27
|
|
pubmed:abstractText |
The design and DNA binding activity of beta-structure-forming peptides and netropsin-peptide conjugates are reported. It is found that a pair of peptides-S,S'-bis(Lys-Gly-Val-Cys-Val-NH-NH-Dns)-bridged by an S-S bond binds at least 10 times more strongly to poly(dG).poly(dC) than to poly(dA).poly(dT). This peptide can also discriminate between 5'-GpG-3' and 5'-GpC-3' steps in the DNA minor groove. Based on these observations, new synthetic ligands, bis-netropsins, were constructed in which two netropsin-like fragments were attached by means of short linkers to a pair of peptides-Gly-Cys-Gly- or Val-Cys-Val-bridged by S-S bonds. These compounds possess a composite binding specificity: the peptide chains recognize 5'-GpG-3' steps on DNA, whereas the netropsin-like fragments bind preferentially to runs of 4 AT base pairs. Our data indicate that combining the AT-base-pair specific properties of the netropsin-type structure with the 5'-GpG-3'-specific properties of certain oligopeptides offers a new approach to the synthesis of ligands capable of recognizing mixed sequences of AT- and GC-base pairs in the DNA minor groove. These compounds are potential models for DNA-binding domains in proteins which specifically recognize base pair sequences in the minor groove of DNA.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aminoglycosides,
http://linkedlifedata.com/resource/pubmed/chemical/Antibiotics, Antineoplastic,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease I,
http://linkedlifedata.com/resource/pubmed/chemical/Distamycins,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Netropsin,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/bis-netropsin,
http://linkedlifedata.com/resource/pubmed/chemical/sibiromycin,
http://linkedlifedata.com/resource/pubmed/chemical/stallimycin
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
0739-1102
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
14
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
31-47
|
|
pubmed:dateRevised |
2007-11-14
|
|
pubmed:meshHeading |
pubmed-meshheading:8877560-Aminoglycosides,
pubmed-meshheading:8877560-Antibiotics, Antineoplastic,
pubmed-meshheading:8877560-Base Composition,
pubmed-meshheading:8877560-Base Sequence,
pubmed-meshheading:8877560-Binding, Competitive,
pubmed-meshheading:8877560-Binding Sites,
pubmed-meshheading:8877560-Cysteine,
pubmed-meshheading:8877560-DNA,
pubmed-meshheading:8877560-Deoxyribonuclease I,
pubmed-meshheading:8877560-Dinucleotide Repeats,
pubmed-meshheading:8877560-Distamycins,
pubmed-meshheading:8877560-Disulfides,
pubmed-meshheading:8877560-Drug Design,
pubmed-meshheading:8877560-Models, Chemical,
pubmed-meshheading:8877560-Models, Molecular,
pubmed-meshheading:8877560-Molecular Sequence Data,
pubmed-meshheading:8877560-Netropsin,
pubmed-meshheading:8877560-Nucleic Acid Conformation,
pubmed-meshheading:8877560-Peptides,
pubmed-meshheading:8877560-Protein Binding,
pubmed-meshheading:8877560-Protein Conformation,
pubmed-meshheading:8877560-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:8877560-Structure-Activity Relationship,
pubmed-meshheading:8877560-Substrate Specificity,
pubmed-meshheading:8877560-Thermodynamics
|
|
pubmed:year |
1996
|
|
pubmed:articleTitle |
Design of sequence-specific DNA binding ligands that use a two-stranded peptide motif for DNA sequence recognition.
|
|
pubmed:affiliation |
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
