Translational and Rotational Motions of Albumin Sensed by a Non-covalent Associated Porphyrin Under Physiological and Acidic Conditions: a Fluorescence Correlation Spectroscopy and Time Resolved Anisotropy Study

Overview

Journal J Fluoresc

Specialties Biophysics
Chemistry

Date 2008 Feb 12

PMID 18264814

Citations 1

Authors

Suzana M Andrade

Silvia M B Costa

Jan Willem Borst

Arie van Hoek

Antonie J W G Visser

Affiliations

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Abstract

The interaction between a free-base, anionic water-soluble porphyrin, TSPP, and the drug carrier protein, bovine serum albumin (BSA) has been studied by time-resolved fluorescence anisotropy (TRFA) and fluorescence correlation spectroscopy (FCS) at two different pH-values. Both rotational correlation times and translational diffusion times of the fluorescent species indicate that TSPP binding to albumin induces very little conformational changes in the protein under physiological conditions. By contrast, at low pH, a bi-exponential decay is obtained where a short rotational correlation time (phi (int) = 1.2 ns) is obtained, which is likely associated to wobbling movement of the porphyrin in the protein binding site. These physical changes are corroborated by circular dichroism (CD) data which show a 37% loss in the protein helicity upon acidification of the medium. In the presence of excess porphyrin formation of porphyrin J-aggregates is induced, which can be detected by time-resolved fluorescence with short characteristic times. This is also reflected in FCS data by an increase in molecular brightness together with a decrease in the number of fluorescent molecules passing through the detection volume of the sample.

Citing Articles

Fluorescence Spectroscopy of Porphyrins and Phthalocyanines: Some Insights into Supramolecular Self-Assembly, Microencapsulation, and Imaging Microscopy.

Teixeira R, Serra V, Botequim D, Paulo P, Andrade S, Costa S Molecules. 2021; 26(14).

PMID: 34299539 PMC: 8306603. DOI: 10.3390/molecules26144264.

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