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Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA
Indolicidin, a l3-residue antimicrobial peptide-amide, which is unusually rich in tryptophan and proline, is isolated from the cytoplasmic granules of bovine neutrophils. In this study, the structures of indolicidin in 50% D(3)-trifluoroethanol and in the absence and presence of SDS and D(38)-dodecy...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2005
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1179735/ https://www.ncbi.nlm.nih.gov/pubmed/16034027 http://dx.doi.org/10.1093/nar/gki725 |
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author | Hsu, Chun-Hua Chen, Chinpan Jou, Maou-Lin Lee, Alan Yueh-Luen Lin, Yu-Ching Yu, Yi-Ping Huang, Wei-Ting Wu, Shih-Hsiung |
author_facet | Hsu, Chun-Hua Chen, Chinpan Jou, Maou-Lin Lee, Alan Yueh-Luen Lin, Yu-Ching Yu, Yi-Ping Huang, Wei-Ting Wu, Shih-Hsiung |
author_sort | Hsu, Chun-Hua |
collection | PubMed |
description | Indolicidin, a l3-residue antimicrobial peptide-amide, which is unusually rich in tryptophan and proline, is isolated from the cytoplasmic granules of bovine neutrophils. In this study, the structures of indolicidin in 50% D(3)-trifluoroethanol and in the absence and presence of SDS and D(38)-dodecylphosphocholine were determined using NMR spectroscopy. Multiple conformations were found and were shown to be due to different combinations of contact between the two WPW motifs. Although indolicidin is bactericidal and able to permeabilize bacterial membranes, it does not lead to cell wall lysis, showing that there is more than one mechanism of antimicrobial action. The structure of indolicidin in aqueous solution was a globular and amphipathic conformation, differing from the wedge shape adopted in lipid micelles, and these two structures were predicted to have different functions. Indolicidin, which is known to inhibit DNA synthesis and induce filamentation of bacteria, was shown to bind DNA in gel retardation and fluorescence quenching experiments. Further investigations using surface plasmon resonance confirmed the DNA-binding ability and showed the sequence preference of indolicidin. Based on our biophysical studies and previous results, we present a diagram illustrating the DNA-binding mechanism of the antimicrobial action of indolicidin and explaining the roles of the peptide when interacting with lipid bilayers at different concentrations. |
format | Text |
id | pubmed-1179735 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-11797352005-07-22 Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA Hsu, Chun-Hua Chen, Chinpan Jou, Maou-Lin Lee, Alan Yueh-Luen Lin, Yu-Ching Yu, Yi-Ping Huang, Wei-Ting Wu, Shih-Hsiung Nucleic Acids Res Article Indolicidin, a l3-residue antimicrobial peptide-amide, which is unusually rich in tryptophan and proline, is isolated from the cytoplasmic granules of bovine neutrophils. In this study, the structures of indolicidin in 50% D(3)-trifluoroethanol and in the absence and presence of SDS and D(38)-dodecylphosphocholine were determined using NMR spectroscopy. Multiple conformations were found and were shown to be due to different combinations of contact between the two WPW motifs. Although indolicidin is bactericidal and able to permeabilize bacterial membranes, it does not lead to cell wall lysis, showing that there is more than one mechanism of antimicrobial action. The structure of indolicidin in aqueous solution was a globular and amphipathic conformation, differing from the wedge shape adopted in lipid micelles, and these two structures were predicted to have different functions. Indolicidin, which is known to inhibit DNA synthesis and induce filamentation of bacteria, was shown to bind DNA in gel retardation and fluorescence quenching experiments. Further investigations using surface plasmon resonance confirmed the DNA-binding ability and showed the sequence preference of indolicidin. Based on our biophysical studies and previous results, we present a diagram illustrating the DNA-binding mechanism of the antimicrobial action of indolicidin and explaining the roles of the peptide when interacting with lipid bilayers at different concentrations. Oxford University Press 2005 2005-07-20 /pmc/articles/PMC1179735/ /pubmed/16034027 http://dx.doi.org/10.1093/nar/gki725 Text en © The Author 2005. Published by Oxford University Press. All rights reserved |
spellingShingle | Article Hsu, Chun-Hua Chen, Chinpan Jou, Maou-Lin Lee, Alan Yueh-Luen Lin, Yu-Ching Yu, Yi-Ping Huang, Wei-Ting Wu, Shih-Hsiung Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA |
title | Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA |
title_full | Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA |
title_fullStr | Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA |
title_full_unstemmed | Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA |
title_short | Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA |
title_sort | structural and dna-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and dna |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1179735/ https://www.ncbi.nlm.nih.gov/pubmed/16034027 http://dx.doi.org/10.1093/nar/gki725 |
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