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An environmental-sensitive BODIPY®-derivative with bioapplication: spectral and photophysical properties
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Medicine, Medical Biochemistry and Biophsyics.
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2003 (English)In: Journal of Fluorescence, ISSN 1053-0509 (Print) 1573-4994 (Online), Vol. 13, no 5, 379-84 p.Article in journal (Refereed) Published
Abstract [en]

A previously synthesised derivative of BODIPY aimed for sulfhydryl specific labelling of cysteine residues in proteins was studied. The spectral and photophysical properties of this derivative, N-(4,4-difluoro-1,3,5,7-tetramethyl-4-bora-3a,4a-diaza-s-indacene-2-yl) iodoacetamide (NBDY) were characterised, and found to be considerably different from those of commonly used derivatives of BODIPY, e.g. N-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-yl)methyl iodoacetamide. The absorption and fluorescence spectra, as well as fluorescence lifetimes and quantum yields of NBDY are quite sensitive to solvent properties. The fluorescence is effectively quenched by I– when NBDY is free in water or attached to Cys in different mutants of plasminogen activator inhibitor type 2 (PAI-2). A ground-state dimer forms when two NBDY groups are closely spaced in plasminogen activator inhibitor type 1 (PAI-1).

Place, publisher, year, edition, pages
2003. Vol. 13, no 5, 379-84 p.
Keyword [en]
BODIPY, donor–donor energy migration, homotransfer, dimers, quenching
Identifiers
URN: urn:nbn:se:umu:diva-10060DOI: doi:10.1023/A:1026156605013OAI: oai:DiVA.org:umu-10060DiVA: diva2:149731
Available from: 2008-06-12 Created: 2008-06-12 Last updated: 2009-10-23Bibliographically approved
In thesis
1. On the quantitative analysis of electronic energy transfer/migration in proteins studied by fluorescence spectroscopy
Open this publication in new window or tab >>On the quantitative analysis of electronic energy transfer/migration in proteins studied by fluorescence spectroscopy
2007 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Two recently developed theories of electronic energy transfer/migration were for the first time applied to real protein systems for extracting molecular distances. The partial donor-donor energy migration (PDDEM) is an extension to the previously developed donor-donor energy migration (DDEM, F Bergström et al PNAS 96, 1999, 12477) which allows using chemically identical but photophysically different fluorophores in energy migration experiments. A method based on fluorescence quenching was investigated and applied to create an asymmetric energy migration between fluorophores which were covalently and specifically attached to plasminogen activator inhibitor type 2 (PAI-2). It was also shown experimentally that distance information can be obtained if the fluorescence relaxation for photophysically identical donors, exhibits multi-exponential relaxation.

An extended Förster theory (EFT) that was previously derived (L. B.-Å. Johansson et al J. Chem. Phys., 1996, 105) ha been developed for analysis of donor-acceptor energy transfer systems as well as DDEM systems. Recently the EFT was also applied to determine intra molecular distances in the protein plasminogen activator inhibitor type 1 (PAI-1) which was labelled with a sulfhydryl specific derivative of BODIPY. The EFT explicitly accounts for the time-dependent reorientations which in a complex manner influence the rate of electronic energy transfer/migration. This difficulty is related to the “k2-problem”, which has been solved. It is also shown experimentally that the time-correlated single-photon counting (TCSPC) data is sensitive to the mutual configuration between the interacting fluorophores. To increase the accuracy in the extracted parameters it is furthermore suggested to collect the fluorescence data under various physico-chemical conditions. It was also shown that the Förster theory is only valid in the initial part of the fluorescence decay.

Place, publisher, year, edition, pages
Umeå: Kemi, 2007. 46 p.
Keyword
Biophysical Chemistry
National Category
Physical Chemistry
Identifiers
urn:nbn:se:umu:diva-1009 (URN)978-91-7264-263-8 (ISBN)
Public defence
2007-03-02, KBC3A9, KBC-huset, 901 87, Umeå, 10:30 (English)
Opponent
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Available from: 2007-02-15 Created: 2007-02-15 Last updated: 2009-10-28Bibliographically approved

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Ny, TorJohansson, Lennart B-Å

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