Two-Photon Macromolecular Probe Based on a Quadrupolar Anthracenyl Scaffold for Sensitive Recognition of Serum Proteins under Simulated Physiological Conditions.

ABSTRACT: The binding interaction of a biocompatible water-soluble polycationic two-photon fluorophore (Ant-PIm) toward human serum albumin (HSA) was thoroughly investigated under simulated physiological conditions using a combination of steady-state, time-resolved, and two-photon excited fluorescence techniques. The emission properties of both Ant-PIm and the fluorescent amino acid residues in HSA undergo remarkable changes upon complexation allowing the thermodynamic profile associated with Ant-PIm-HSA complexation to be accurately established. The marked increase in Ant-PIm fluorescence intensity and quantum yield in the proteinous environment seems to be the outcome of the attenuation of radiationless decay pathways resulting from motional restriction imposed on the f

SUBMITTER: Deiana M 

PROVIDER: S-EPMC6045344 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature