In:
Applied Spectroscopy, SAGE Publications, Vol. 70, No. 10 ( 2016-10), p. 1733-1738
Abstract:
In this paper, we report a pyridinium salt “turn-on” fluorescent probe, 4-[2-(4-Dimethylamino-phenyl)-vinyl]-1-methylpyridinium iodide (p-DASPMI), and applied its time-resolved fluorescence (TRF) to monitor the protein conformational changes. Both the fluorescence lifetime and quantum yield (QY) of p-DASPMI were increased about two orders of magnitude after binding to the protein bovine serum albumin (BSA). The free p-DASPMI in solution presents an ultrashort fluorescence lifetime (12.4 ps), thus it does not interfere the detection of bound p-DASPMI which has nanosecond fluorescence lifetime. Decay-associated spectra (DAS) show that p-DASPMI molecules bind to subdomains IIA and IIIA of BSA. The TRF decay profiles of p-DASPMI can be described by the multi-exponential decay function ([Formula: see text]), and the obtained parameters, such as lifetimes ([Formula: see text] ), fractional amplitudes ([Formula: see text]), and fractional intensities ([Formula: see text] ), may be used to deduce the conformational changes of BSA. The pH and Cu 2+ induced conformational changes of BSA were investigated through the TRF of p-DASPMI. The results show that the p-DASPMI is a candidate fluorescent probe in studying the conformational changes of proteins through TRF spectroscopy and microscopy in the visible range.
Type of Medium:
Online Resource
ISSN:
0003-7028
,
1943-3530
DOI:
10.1177/0003702816644609
Language:
English
Publisher:
SAGE Publications
Publication Date:
2016
detail.hit.zdb_id:
1474251-2
detail.hit.zdb_id:
204667-2
SSG:
11
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