Tryptophan Fluorescence in HDL3 with Ferrous Ions

The change in secondary structure upon treatment with ferrous ions was observed at the WMF of the tryptophan residues in HDL₃. The WMF was determined from the uncorrected spectra obtained on an FL6500 spectrofluorometer (Perkin–Elmer, Norwalk, CT, USA) using Spectrum FL software version 1.2.0.583 (Perkin–Elmer) and a 1 cm path-length Suprasil quartz cuvette (Fisher Scientific, Pittsburgh, PA, USA). The samples were excited at 295 nm to avoid tyrosine fluorescence. As described previously, the emission spectra were scanned from 305 to 400 nm at room temperature [56 (link)].

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Cho K.H., Nam H.S., Kim J.E., Na H.J., del Carmen Dominguez-Horta M, & Martinez-Donato G. (2023). CIGB-258 Exerts Potent Anti-Inflammatory Activity against Carboxymethyllysine-Induced Acute Inflammation in Hyperlipidemic Zebrafish via the Protection of Apolipoprotein A-I. International Journal of Molecular Sciences, 24(8), 7044.

Publication 2023

FL6500 spectrofluorometer Spectrum FL software Suprasil quartz cuvette

Fluorescence Hdl3 Ions Nm 295 Quartz Tryptophan Tyrosine

Corresponding Organization : Yeungnam University

Other organizations : Centro de Ingeniería Genética y Biotecnología

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Variable analysis

independent variables

Treatment with ferrous ions

dependent variables

Change in secondary structure of HDL3

control variables

Tryptophan residues in HDL3
Excitation wavelength of 295 nm
Emission spectra scanned from 305 to 400 nm
Room temperature

controls

No positive or negative controls were explicitly mentioned.

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