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Variation of the intercalating proline in artificial peptides mimicking the DNA binding and bending IHF protein
The integration host factor (IHF) is a protein which sequence specifically induces a bend of double-stranded DNA by more than 160°. Based on IHF as lead structure, a peptide mimic was introduced resembling the positively charged body of the protein by a lysine dendrimer and the minor groove recognit...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Vienna
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3374092/ https://www.ncbi.nlm.nih.gov/pubmed/21922266 http://dx.doi.org/10.1007/s00726-011-1073-1 |
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author | Scholz, S. Liebler, E. K. Eickmann, B. Fritz, H.-J. Diederichsen, U. |
author_facet | Scholz, S. Liebler, E. K. Eickmann, B. Fritz, H.-J. Diederichsen, U. |
author_sort | Scholz, S. |
collection | PubMed |
description | The integration host factor (IHF) is a protein which sequence specifically induces a bend of double-stranded DNA by more than 160°. Based on IHF as lead structure, a peptide mimic was introduced resembling the positively charged body of the protein by a lysine dendrimer and the minor groove recognition loop by a cyclopeptide. The proline located close to the tip of the recognition loop intercalates between the base pair plane. It was modified in order to evaluate the influence of the side chain residue with respect to size (1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid), aromaticity (phenylalanine), conformation of the five-membered ring [(4R)-fluoroproline, (4S)-fluoroproline, 3,4-dehydroproline], and the peptide backbone conformation (α-methylproline) on binding dsDNA and bending the double strand. Binding and bending studies were carried out by fluorescence resonance energy transfer experiments and gel electrophoresis using DNA sequences prepared by PCR with the IHF binding site in central or terminal position. Whereas aromatic residues and α-methylproline were not tolerated as proline substitute, incorporation of (4S)-fluoroproline and 3,4-dehydroproline provided enhanced binding. |
format | Online Article Text |
id | pubmed-3374092 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Springer Vienna |
record_format | MEDLINE/PubMed |
spelling | pubmed-33740922012-06-14 Variation of the intercalating proline in artificial peptides mimicking the DNA binding and bending IHF protein Scholz, S. Liebler, E. K. Eickmann, B. Fritz, H.-J. Diederichsen, U. Amino Acids Original Article The integration host factor (IHF) is a protein which sequence specifically induces a bend of double-stranded DNA by more than 160°. Based on IHF as lead structure, a peptide mimic was introduced resembling the positively charged body of the protein by a lysine dendrimer and the minor groove recognition loop by a cyclopeptide. The proline located close to the tip of the recognition loop intercalates between the base pair plane. It was modified in order to evaluate the influence of the side chain residue with respect to size (1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid), aromaticity (phenylalanine), conformation of the five-membered ring [(4R)-fluoroproline, (4S)-fluoroproline, 3,4-dehydroproline], and the peptide backbone conformation (α-methylproline) on binding dsDNA and bending the double strand. Binding and bending studies were carried out by fluorescence resonance energy transfer experiments and gel electrophoresis using DNA sequences prepared by PCR with the IHF binding site in central or terminal position. Whereas aromatic residues and α-methylproline were not tolerated as proline substitute, incorporation of (4S)-fluoroproline and 3,4-dehydroproline provided enhanced binding. Springer Vienna 2011-09-16 2012 /pmc/articles/PMC3374092/ /pubmed/21922266 http://dx.doi.org/10.1007/s00726-011-1073-1 Text en © The Author(s) 2011 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited. |
spellingShingle | Original Article Scholz, S. Liebler, E. K. Eickmann, B. Fritz, H.-J. Diederichsen, U. Variation of the intercalating proline in artificial peptides mimicking the DNA binding and bending IHF protein |
title | Variation of the intercalating proline in artificial peptides mimicking the DNA binding and bending IHF protein |
title_full | Variation of the intercalating proline in artificial peptides mimicking the DNA binding and bending IHF protein |
title_fullStr | Variation of the intercalating proline in artificial peptides mimicking the DNA binding and bending IHF protein |
title_full_unstemmed | Variation of the intercalating proline in artificial peptides mimicking the DNA binding and bending IHF protein |
title_short | Variation of the intercalating proline in artificial peptides mimicking the DNA binding and bending IHF protein |
title_sort | variation of the intercalating proline in artificial peptides mimicking the dna binding and bending ihf protein |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3374092/ https://www.ncbi.nlm.nih.gov/pubmed/21922266 http://dx.doi.org/10.1007/s00726-011-1073-1 |
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