Splitting and self-assembling of far-red fluorescent protein with an engineered beta strand peptide: Application for alpha-synuclein imaging in mammalian cells

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dc.contributor.authorJoo Oak Keem-
dc.contributor.authorIn Hwan Lee-
dc.contributor.authorSun Young Kim-
dc.contributor.authorYongwon Jung-
dc.contributor.authorBong Hyun Chung-
dc.date.accessioned2017-04-19T09:25:17Z-
dc.date.available2017-04-19T09:25:17Z-
dc.date.issued2011-
dc.identifier.issn0142-9612-
dc.identifier.uri10.1016/j.biomaterials.2011.08.029ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10307-
dc.description.abstractWe introduce the strategic development of self-assembling peptide/protein fragments based on the far-red fluorescent protein mPlum. The first beta strand (mPlum 1, 18 amino acids) of mPlum was engineered to spontaneously bind with the rest of the protein (mPlum 2-11, next 10 beta strands) and to form a native chromophore. The target beta strand mPlum 1 was separated from mPlum 2-11 and linked via a flexible peptide linker, resulting in fluorescently inactive circularly permuted mPlum protein (CpmPlum). In vitro evolution of this CpmPlum to a fluorescently active form and the subsequent splitting of the engineered mPlum 1 peptide afforded self-assembling mPlum fragments. Recombinantly expressed and synthetically prepared beta strand peptides were successfully assembled with the remaining mPlum protein in vitro and in cells. This developed pair of peptide/protein fragments was effectively used for peptide tag detection of alpha-synuclein in mammalian cells. Sequential expression of self-assembling mPlum fragments offered an entirely genetically encoded sensing system of naturally unfolded alpha-synuclein.-
dc.publisherElsevier-
dc.titleSplitting and self-assembling of far-red fluorescent protein with an engineered beta strand peptide: Application for alpha-synuclein imaging in mammalian cells-
dc.title.alternativeSplitting and self-assembling of far-red fluorescent protein with an engineered beta strand peptide: Application for alpha-synuclein imaging in mammalian cells-
dc.typeArticle-
dc.citation.titleBiomaterials-
dc.citation.number34-
dc.citation.endPage9058-
dc.citation.startPage9051-
dc.citation.volume32-
dc.contributor.affiliatedAuthorJoo Oak Keem-
dc.contributor.affiliatedAuthorIn Hwan Lee-
dc.contributor.affiliatedAuthorSun Young Kim-
dc.contributor.affiliatedAuthorYongwon Jung-
dc.contributor.affiliatedAuthorBong Hyun Chung-
dc.contributor.alternativeName김주옥-
dc.contributor.alternativeName이인환-
dc.contributor.alternativeName김선영-
dc.contributor.alternativeName정용원-
dc.contributor.alternativeName정봉현-
dc.identifier.bibliographicCitationBiomaterials, vol. 32, no. 34, pp. 9051-9058-
dc.identifier.doi10.1016/j.biomaterials.2011.08.029-
dc.subject.keywordBiosensors-
dc.subject.keywordFluorescent protein-
dc.subject.keywordMolecular evolution-
dc.subject.keywordProtein engineering-
dc.subject.keywordSplit protein-
dc.subject.localbiosensor-
dc.subject.localBio-sensor-
dc.subject.localBiosensor-
dc.subject.localbiosensors-
dc.subject.localBiosensors-
dc.subject.localFluorescent protein-
dc.subject.localFluorescent proteins-
dc.subject.localMolecular evolution-
dc.subject.localmolecular evolution-
dc.subject.localProtein engineering-
dc.subject.localprotein engineering-
dc.subject.localProtein Engineering-
dc.subject.localSplit protein-
dc.description.journalClassY-
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