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Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation
dc.creator | Milošević, Jelica | |
dc.creator | Petrić, Jovan | |
dc.creator | Jovčić, Branko | |
dc.creator | Janković, Brankica | |
dc.creator | Polović, Natalija | |
dc.date.accessioned | 2020-03-31T19:16:12Z | |
dc.date.available | 2021-11-30 | |
dc.date.issued | 2020 | |
dc.identifier.issn | 1386-1425 | |
dc.identifier.uri | https://cherry.chem.bg.ac.rs/handle/123456789/3895 | |
dc.description.abstract | Amyloid fibrils are highly ordered self-assembled (poly)peptide aggregates with cross-β structural pattern. Ovalbumin was used as a model for exploring the potential of infrared spectroscopy in detecting structural transitions and quantitative monitoring of amyloid fibrillation. Low pH (pH 2) and high temperature (90 °C) over the course of 24 h were conditions applied for amyloid formation. Fibrillation of ovalbumin was monitored by ThT and ANS fluorescence, and SDS PAGE. A significant increase in ThT fluorescence with a plateau reached after 4 h of incubation, without the lag phase, was detected. Structural transitions leading to amyloid fibrillation were analysed using all three Amide regions in ATR-FTIR spectra. Significant changes were detected in Amide I and Amide III region (decrease of α-helix and increase of β-sheet peaks). To establish a fast, precise and simple method for quantitative monitoring of amyloid fibrillation, the Amide I/Amide II ratios of aggregation specific β-sheets (1625 and 1695 cm−1, respectively) with 1540 cm−1 as internal standard were used, resulting in good correlation (R2 = 0.93 and 0.95) with the data observed by monitoring ThT fluorescence. On the other hand, assessing aggregation specific β-sheet contents by self-deconvolution showed lower correlation with ThT fluorescence (R2 = 0.75 and 0.64). Here we examined structural transitions during ovalbumin fibrillation in a qualitative and quantitative manner by exploiting the full potential of Amide regions simultaneously. Secondary structure distribution was monitored using second derivative spectra in Amide I region. A novel, simple mathematical calculation for quantitative monitoring of fibrils formation was presented employing that the increase in low and high frequency aggregation specific β-sheet in Amide I region compared to the internal standard in Amide II region is suitable for fibril formation monitoring. | |
dc.publisher | Elsevier | |
dc.relation | info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172049/RS// | |
dc.rights | embargoedAccess | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/4.0/ | |
dc.source | Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy | |
dc.subject | Amide I/Amide II ratio | |
dc.subject | Amyloid fibrils | |
dc.subject | ATR-FTIR | |
dc.subject | Ovalbumin | |
dc.subject | Secondary structures | |
dc.title | Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation | |
dc.type | article | |
dc.rights.license | BY-NC-ND | |
dcterms.abstract | Петрић, Јован; Јанковић, Бранкица; Половић, Наталија; Јовчић, Бранко; Милошевић, Јелица; | |
dc.citation.volume | 229 | |
dc.identifier.wos | 000513007800040 | |
dc.identifier.doi | 10.1016/j.saa.2019.117882 | |
dc.citation.rank | M21~ | |
dc.description.other | This is the peer-reviewed version of the article: (1) Milošević, J.; Petrić, J.; Jovčić, B.; Janković, B.; Polović, N. Exploring the Potential of Infrared Spectroscopy in Qualitative and Quantitative Monitoring of Ovalbumin Amyloid Fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 2020, 229. [https://doi.org/10.1016/j.saa.2019.117882] | |
dc.description.other | Supplementary material: [http://cherry.chem.bg.ac.rs/handle/123456789/3894] | |
dc.type.version | acceptedVersion | |
dc.identifier.scopus | 2-s2.0-85076245100 | |
dc.identifier.fulltext | http://cherry.chem.bg.ac.rs/bitstream/id/16859/Exploring_the_potential_acc_2020.pdf |