@article{Lux2021Amylo-51937,
  year={2021},
  doi={10.1016/j.foodhyd.2020.106174},
  title={Amyloid aggregation of spin-labeled β-lactoglobulin. Part II : Identification of spin-labeled protein and peptide sequences after amyloid aggregation},
  volume={112},
  issn={0268-005X},
  journal={Food Hydrocolloids},
  author={Lux, Jacqueline and Azarkh, Mykhailo and Fitzner, Laura and Keppler, Julia K. and Schwarz, Karin and Drescher, Malte and Steffen-Heins, Anja},
  note={Article Number: 106174}
}

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    <dc:contributor>Drescher, Malte</dc:contributor>
    <dc:contributor>Fitzner, Laura</dc:contributor>
    <dc:contributor>Azarkh, Mykhailo</dc:contributor>
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    <dcterms:issued>2021</dcterms:issued>
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    <dc:creator>Steffen-Heins, Anja</dc:creator>
    <dc:language>eng</dc:language>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2020-11-27T08:20:15Z</dcterms:available>
    <dcterms:abstract xml:lang="eng">Site-directed spin labeling (SDSL) of natural β-lactoglobulin (β-lg) was established. Combined electron paramagnetic resonance (EPR) and mass spectrometric analysis following tryptic digestion demonstrated that spin labels bind site-specifically but are not directed to all five cysteine residues to various preferred and reproducible extents. MTSSL and iodoacetamido-proxyl spin label (IPSL) were 80 and 60% reliably bound to the H strand, respectively, and combined in one spectral component and buried in the protein core. After heat incubation at pH 2 and fractionation, all labeled side chains (peptides) were part of the amyloid and non-amyloid fractions, even if they could not detect amyloid structures. It was assumed that the IPSL-labeled side chains of peptides with Cys160 from random coil were incorporated into small non-amyloid aggregates in non-polar environments. After heating at pH 3.5, a rearrangement of the previous α-helix was assumed to shift from the autonomous folding domain during partial unfolding, which improved the accessibility of β-sheets to the water/DMSO-environment. β-sheets were likely densely packed by the accumulation of intermolecular β-sheets, which suggests that amyloid-like structures can be formed from building blocks of the entire primary β-lg structure. Double electron-electron resonance (DEER) confirmed that the spatial distribution of labels within the amyloid-like fraction in a one-dimensional arrangement of the entire protein aggregates was similar to a string of pearls. Thus, SDSL of proteins containing several cysteine residues can be used to gain deep insights into the aggregation mechanism of proteins under food processing conditions.</dcterms:abstract>
    <dc:contributor>Steffen-Heins, Anja</dc:contributor>
    <dc:creator>Keppler, Julia K.</dc:creator>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2020-11-27T08:20:15Z</dc:date>
    <dcterms:title>Amyloid aggregation of spin-labeled β-lactoglobulin. Part II : Identification of spin-labeled protein and peptide sequences after amyloid aggregation</dcterms:title>
    <dc:creator>Schwarz, Karin</dc:creator>
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    <dc:creator>Azarkh, Mykhailo</dc:creator>
    <dc:creator>Lux, Jacqueline</dc:creator>
    <dc:contributor>Schwarz, Karin</dc:contributor>
    <dc:creator>Drescher, Malte</dc:creator>
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    <dc:contributor>Lux, Jacqueline</dc:contributor>
    <dc:contributor>Keppler, Julia K.</dc:contributor>
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    <dc:creator>Fitzner, Laura</dc:creator>
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