1. Interaction of the iron(II) cage complexes with proteins: protein fluorescence quenching study.
- Author
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Losytskyy MY, Kovalska VB, Varzatskii OA, Sergeev AM, Yarmoluk SM, and Voloshin YZ
- Subjects
- Animals, Cattle, Molecular Conformation, Muramidase metabolism, Spectrometry, Fluorescence, Ferrous Compounds chemistry, Fluorescence, Insulin chemistry, Lactoglobulins chemistry, Muramidase chemistry, Serum Albumin, Bovine chemistry
- 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.
- Published
- 2013
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