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Interaction of the iron(II) cage complexes with proteins: protein fluorescence quenching study.
- Source :
-
Journal of fluorescence [J Fluoresc] 2013 Sep; Vol. 23 (5), pp. 889-95. Date of Electronic Publication: 2013 Apr 04. - Publication Year :
- 2013
-
Abstract
- Interaction of the iron(II) mono- and bis-clathrochelates with bovine serum albumin (BSA), β-lactoglobulin, lysozyme and insulin was studied by the steady-state and time-resolved fluorescent spectroscopies. These cage complexes do not make significant impact on fluorescent properties of β-lactoglobulin, lysozyme and insulin. At the same time, the monoclathrochelates strongly quench a fluorescence intensity of BSA and substantially decrease its excited state lifetime due to their binding to this protein. This occurs due to the excitation energy transfer from a tryptophan residue to a cage molecule or/and to the change of the tryptophan nearest environment caused by either clathrochelate binding or an alteration of the BSA conformation. The effect of the iron(II) bis-clathrochelate on BSA fluorescence is much weaker as compared to its monomacrobicyclic analogs as a result of an increase in its size.
Details
- Language :
- English
- ISSN :
- 1573-4994
- Volume :
- 23
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Journal of fluorescence
- Publication Type :
- Academic Journal
- Accession number :
- 23553641
- Full Text :
- https://doi.org/10.1007/s10895-013-1199-5