dc.date.accessioned | 2021-03-15T19:48:44Z | |
dc.date.available | 2021-03-15T19:48:44Z | |
dc.date.created | 2020-11-19T21:08:46Z | |
dc.date.issued | 2020 | |
dc.identifier.citation | Molchanova, Natalia Nielsen, Josefine Eilsø Sørensen, Kristian B Krishna, Bala Hansen, Paul Robert Lund, Reidar Barron, Annelise E. Jenssen, Håvard . Halogenation as a tool to tune antimicrobial activity of peptoids. Scientific Reports. 2020, 10(1) | |
dc.identifier.uri | http://hdl.handle.net/10852/84083 | |
dc.description.abstract | Abstract
Antimicrobial peptides have attracted considerable interest as potential new class of antibiotics against multi-drug resistant bacteria. However, their therapeutic potential is limited, in part due to susceptibility towards enzymatic degradation and low bioavailability. Peptoids (oligomers of N -substituted glycines) demonstrate proteolytic stability and better bioavailability than corresponding peptides while in many cases retaining antibacterial activity. In this study, we synthesized a library of 36 peptoids containing fluorine, chlorine, bromine and iodine atoms, which vary by length and level of halogen substitution in position 4 of the phenyl rings. As we observed a clear correlation between halogenation of an inactive model peptoid and its increased antimicrobial activity, we designed chlorinated and brominated analogues of a known peptoid and its shorter counterpart. Short brominated analogues displayed up to 32-fold increase of the activity against S. aureus and 16- to 64-fold against E. coli and P. aeruginosa alongside reduced cytotoxicity. The biological effect of halogens seems to be linked to the relative hydrophobicity and self-assembly properties of the compounds. By small angle X-ray scattering (SAXS) we have demontrated how the self-assembled structures are dependent on the size of the halogen, degree of substitution and length of the peptoid, and correlated these features to their activity. | |
dc.language | EN | |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.title | Halogenation as a tool to tune antimicrobial activity of peptoids | |
dc.type | Journal article | |
dc.creator.author | Molchanova, Natalia | |
dc.creator.author | Nielsen, Josefine Eilsø | |
dc.creator.author | Sørensen, Kristian B | |
dc.creator.author | Krishna, Bala | |
dc.creator.author | Hansen, Paul Robert | |
dc.creator.author | Lund, Reidar | |
dc.creator.author | Barron, Annelise E. | |
dc.creator.author | Jenssen, Håvard | |
cristin.unitcode | 185,15,12,63 | |
cristin.unitname | Seksjon for kjemisk livsvitenskap - biomolekyler, bio-inspirerte materialer og bioanalytisk kjemi | |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 1 | |
dc.identifier.cristin | 1850107 | |
dc.identifier.bibliographiccitation | info:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Scientific Reports&rft.volume=10&rft.spage=&rft.date=2020 | |
dc.identifier.jtitle | Scientific Reports | |
dc.identifier.volume | 10 | |
dc.identifier.issue | 1 | |
dc.identifier.pagecount | 10 | |
dc.identifier.doi | https://doi.org/10.1038/s41598-020-71771-8 | |
dc.identifier.urn | URN:NBN:no-86799 | |
dc.type.document | Tidsskriftartikkel | |
dc.type.peerreviewed | Peer reviewed | |
dc.source.issn | 2045-2322 | |
dc.identifier.fulltext | Fulltext https://www.duo.uio.no/bitstream/handle/10852/84083/1/s41598-020-71771-8.pdf | |
dc.type.version | PublishedVersion | |
cristin.articleid | 14805 | |