Photobehaviour of 4-trifluoromethyl-1-naphthol within protein microenvironment

Autores UPV
Año
CONGRESO Photobehaviour of 4-trifluoromethyl-1-naphthol within protein microenvironment

Abstract

Human serum albumin (HSA) is a transport protein very abundant in blood and plasma; one of their main functions is to carry endogenous and exogenous agents in the bloodstream.1 Binding of ligands to HSA is a process that can modulate a number of properties of the carried agent. In this work, the photophysical behaviour of 4-trifluoromethyl-1-hydroxy-naphthalene (TFN) 2, 3, 4 encapsulated within HSA is described. Supramolecular binding of TFN to HSA can be followed by the enhancement of the fluorescence emission after addition of increasing amounts of protein (Figure 1A). A complex TFN@HSA is detected in the absorption spectrum with maxima at ca. 340 nm