Ratiometric analyses at critical temperatures can magnify the signal intensity of FRET-based sugar sensors with periplasmic binding proteins = 분석온도 조절을 통한 당 감지 센서의 감지능 향상

Cited 3 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorJongsik Gam-
dc.contributor.authorJae-Seok Ha-
dc.contributor.authorHaseong Kim-
dc.contributor.authorDae-Hee Lee-
dc.contributor.authorJ Lee-
dc.contributor.authorSeung Goo Lee-
dc.date.accessioned2017-04-19T10:05:04Z-
dc.date.available2017-04-19T10:05:04Z-
dc.date.issued2015-
dc.identifier.issn09565663-
dc.identifier.uri10.1016/j.bios.2015.04.083ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/12611-
dc.description.abstractFluorescence resonance energy transfer (FRET)-based sensors transduce ligand recognition into a change in the fluorophore spectrum, as ligand binding alters the distance between and orientation of two fluorescent proteins. Here, we report a dramatic increase in the signal intensity of FRET-based sugar sensors with bacterial periplasmic binding proteins (PBPs) in the binding moiety, by increasing the analysis temperature, usually higher than 50. °C. The increased signal intensity results from a sudden decrease in background signal at critical temperatures, while recovering the maximum FRET ratios in the presence of ligands. When tested with a maltose sensor using a maltose-binding protein as the binding moiety, the FRET ratio at the critical temperature, 55. °C, was 17-fold higher than at ambient temperatures. Similar effects were observed using analogous sensors for allose, arabinose, and glucose, providing highly dynamic and quantitative ratio changes at the critical temperatures. The proposed mechanism underlying the signal improvement is thermal relaxation of the binding proteins at the critical temperature; this hypothesis was supported by the results of intrinsic tryptophan fluorescence and circular dichroism experiments. In summary, this study shows that the conformational relaxation of proteins under specific conditions can be leveraged for highly sensitive and rapid measurements of ligands using FRET-based sensors.-
dc.publisherElsevier-
dc.titleRatiometric analyses at critical temperatures can magnify the signal intensity of FRET-based sugar sensors with periplasmic binding proteins = 분석온도 조절을 통한 당 감지 센서의 감지능 향상-
dc.title.alternativeRatiometric analyses at critical temperatures can magnify the signal intensity of FRET-based sugar sensors with periplasmic binding proteins-
dc.typeArticle-
dc.citation.titleBiosensors & Bioelectronics-
dc.citation.number1-
dc.citation.endPage43-
dc.citation.startPage37-
dc.citation.volume72-
dc.contributor.affiliatedAuthorHaseong Kim-
dc.contributor.affiliatedAuthorDae-Hee Lee-
dc.contributor.affiliatedAuthorSeung Goo Lee-
dc.contributor.alternativeName감종식-
dc.contributor.alternativeName하재석-
dc.contributor.alternativeName김하성-
dc.contributor.alternativeName이대희-
dc.contributor.alternativeName이지연-
dc.contributor.alternativeName이승구-
dc.identifier.bibliographicCitationBiosensors & Bioelectronics, vol. 72, no. 1, pp. 37-43-
dc.identifier.doi10.1016/j.bios.2015.04.083-
dc.subject.keywordConformation relaxation-
dc.subject.keywordCritical temperature-
dc.subject.keywordFluorescence resonance energy transfer-
dc.subject.keywordMolecular biosensor-
dc.subject.localConformation relaxation-
dc.subject.localCritical temperature-
dc.subject.localFluorescence resonance energy transfer-
dc.subject.localFluorescence resonance energy transfer (FRET)-
dc.subject.localMolecular biosensor-
dc.description.journalClassY-
Appears in Collections:
Division of Biomaterials Research > Synthetic Biology and Bioengineering Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.