Blue autofluorescence in protein aggregates lighted on by UV induced oxidation

Valeria Vetri, Anna Fricano, Estella Rao, Librizzi, Anna Fricano, Alfano, Fabio Librizzi

Risultato della ricerca: Article

Abstract

Oxidation of amino acid side chains in protein structure can be induced by UV irradiation leading to critical changes in molecular structure possibly modifying protein stability and bioactivity.Here we show, by using a combination of multiple spectroscopic techniques and Fluorescence Lifetime Imaging, that UV-light exposure induces irreversible oxidation processes in Ubiquitin structure. In particular, the growth of a new autofluorescence peak in the blue region is detected, that we attribute to tyrosine oxidation products. Blue autofluorescence intensity is found to progressively increase also during aggregation processes leading to the formation of aggregates of non-amyloid nature. Significantly, analogous spectral modifications are found in amyloid fibrils from human insulin and Amyloidβ peptide grown under UV exposure. Experimental results reveal a substantial overlap between the fluorescence signal here attributed to tyrosine oxidation and the one referred in literature as “Amyloid autofluorescence”. These findings clearly represent a caveat about the specificity of the blue fluorescence peak measured for amyloids, especially when grown in conditions in which tyrosine residues may be oxidized. Moreover, our results once again highlight the close link between the formation of amyloid aggregates and protein damage resulting from oxidative stress, as these neurotoxic aggregate species are found to contain damaged residues.
Lingua originaleEnglish
pagine (da-a)140258-
Numero di pagine10
RivistaBIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume1867
Stato di pubblicazionePublished - 2019

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Amyloid
Tyrosine
Oxidation
Fluorescence
Amyloidogenic Proteins
Protein Stability
Optical Imaging
Ultraviolet Rays
Ubiquitin
Molecular Structure
Oxidative stress
Bioactivity
Oxidative Stress
Ultraviolet radiation
Molecular structure
Insulin
Amino Acids
Proteins
Agglomeration
Peptides

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology

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Blue autofluorescence in protein aggregates lighted on by UV induced oxidation. / Vetri, Valeria; Fricano, Anna; Rao, Estella; Librizzi; Fricano, Anna; Alfano; Librizzi, Fabio.

In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, Vol. 1867, 2019, pag. 140258-.

Risultato della ricerca: Article

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abstract = "Oxidation of amino acid side chains in protein structure can be induced by UV irradiation leading to critical changes in molecular structure possibly modifying protein stability and bioactivity.Here we show, by using a combination of multiple spectroscopic techniques and Fluorescence Lifetime Imaging, that UV-light exposure induces irreversible oxidation processes in Ubiquitin structure. In particular, the growth of a new autofluorescence peak in the blue region is detected, that we attribute to tyrosine oxidation products. Blue autofluorescence intensity is found to progressively increase also during aggregation processes leading to the formation of aggregates of non-amyloid nature. Significantly, analogous spectral modifications are found in amyloid fibrils from human insulin and Amyloidβ peptide grown under UV exposure. Experimental results reveal a substantial overlap between the fluorescence signal here attributed to tyrosine oxidation and the one referred in literature as “Amyloid autofluorescence”. These findings clearly represent a caveat about the specificity of the blue fluorescence peak measured for amyloids, especially when grown in conditions in which tyrosine residues may be oxidized. Moreover, our results once again highlight the close link between the formation of amyloid aggregates and protein damage resulting from oxidative stress, as these neurotoxic aggregate species are found to contain damaged residues.",
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T1 - Blue autofluorescence in protein aggregates lighted on by UV induced oxidation

AU - Vetri, Valeria

AU - Fricano, Anna

AU - Rao, Estella

AU - Librizzi, null

AU - Fricano, Anna

AU - Alfano, null

AU - Librizzi, Fabio

PY - 2019

Y1 - 2019

N2 - Oxidation of amino acid side chains in protein structure can be induced by UV irradiation leading to critical changes in molecular structure possibly modifying protein stability and bioactivity.Here we show, by using a combination of multiple spectroscopic techniques and Fluorescence Lifetime Imaging, that UV-light exposure induces irreversible oxidation processes in Ubiquitin structure. In particular, the growth of a new autofluorescence peak in the blue region is detected, that we attribute to tyrosine oxidation products. Blue autofluorescence intensity is found to progressively increase also during aggregation processes leading to the formation of aggregates of non-amyloid nature. Significantly, analogous spectral modifications are found in amyloid fibrils from human insulin and Amyloidβ peptide grown under UV exposure. Experimental results reveal a substantial overlap between the fluorescence signal here attributed to tyrosine oxidation and the one referred in literature as “Amyloid autofluorescence”. These findings clearly represent a caveat about the specificity of the blue fluorescence peak measured for amyloids, especially when grown in conditions in which tyrosine residues may be oxidized. Moreover, our results once again highlight the close link between the formation of amyloid aggregates and protein damage resulting from oxidative stress, as these neurotoxic aggregate species are found to contain damaged residues.

AB - Oxidation of amino acid side chains in protein structure can be induced by UV irradiation leading to critical changes in molecular structure possibly modifying protein stability and bioactivity.Here we show, by using a combination of multiple spectroscopic techniques and Fluorescence Lifetime Imaging, that UV-light exposure induces irreversible oxidation processes in Ubiquitin structure. In particular, the growth of a new autofluorescence peak in the blue region is detected, that we attribute to tyrosine oxidation products. Blue autofluorescence intensity is found to progressively increase also during aggregation processes leading to the formation of aggregates of non-amyloid nature. Significantly, analogous spectral modifications are found in amyloid fibrils from human insulin and Amyloidβ peptide grown under UV exposure. Experimental results reveal a substantial overlap between the fluorescence signal here attributed to tyrosine oxidation and the one referred in literature as “Amyloid autofluorescence”. These findings clearly represent a caveat about the specificity of the blue fluorescence peak measured for amyloids, especially when grown in conditions in which tyrosine residues may be oxidized. Moreover, our results once again highlight the close link between the formation of amyloid aggregates and protein damage resulting from oxidative stress, as these neurotoxic aggregate species are found to contain damaged residues.

UR - http://hdl.handle.net/10447/368786

M3 - Article

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SP - 140258-

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

ER -