1997•Collection of Czechoslovak Chemical CommunicationsRequires access

Glycation of Human Serum Albumin by DL-Glyceraldehyde: A Fluorescence Quenching Study

Miroslav Štěpánek, Zdeněk Pavlı́ček

Abstract

Process of glycation of human serum albumin (HSA) by DL-glyceraldehyde was studied using steady-state and time-resolved fluorescence spectroscopy in the course of 100 h. During this period, measurements of steady-state tryptophan (Trp) and non-tryptophan (non-Trp) fluorescence of the glycated HSA were carried out, together with measurement of the non-Trp fluorescence decay and steady-state quenching using potassium iodide as a quencher. Observed changes in both Trp and non-Trp fluorescence intensity, as well as changes in non-Trp fluorescence lifetimes and quenching efficiency are explained with respect to a probable mechanism of glycation.

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Key concepts: Glycation, Chemistry, Fluorescence, Human serum albumin, Tryptophan, Quenching (fluorescence), Iodide, Fluorescence spectroscopy