Heat-Induced Aggregation of Hen Ovalbumin Suggests a Key Factor Responsible for Serpin Polymerization

Biochemistry
Masahiro NojiYuji Goto

Abstract

Although ovalbumin (OVA), a main component of hen egg white and a non-inhibitory serpin superfamily protein, has been reported to form fibrillar aggregates, its relationship with amyloid fibrils associated with various degenerative diseases is unclear. We studied the heat-induced aggregation of intact OVA using an amyloid-specific thioflavin T assay with a fluorometer or direct imaging with a light-emitting diode lamp and several physicochemical approaches, and the results confirmed that intact OVA forms aggregates with a small part of amyloid cores and dominantly amorphous aggregates. We isolated the amyloidogenic core peptide by proteolysis with trypsin. The isolated 23-residue peptide, pOVA, with marked amyloidogenicity, corresponded to one (β-strand 3A) of the key regions involved in serpin latency transition and domain-swap polymerization leading to serpinopathies. Although the strong amyloidogenicity of pOVA was suppressed in a mixture of tryptic digests, it was observed under acidic conditions in the presence of various salts, with which pOVA has a positive charge. Cytotoxicity measurements suggested that, although heat-treated OVA aggregates exhibited the strongest toxicity, it was attributed to a general property of am...Continue Reading

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Citations

Jan 24, 2021·International Journal of Biological Macromolecules·Manjumol MathewUsha K Aravind
Jan 28, 2021·Communications Biology·Masahiro NojiYuji Goto
Feb 1, 2021·International Journal of Biological Macromolecules·Shoyab AnsariMohamad Aman Jairajpuri
Jan 20, 2020·Trends in Biotechnology·Priyank SinghviAmulya K Panda
Mar 8, 2021·The Journal of Biological Chemistry·Keiichi YamaguchiYuji Goto
Apr 10, 2020·Langmuir : the ACS Journal of Surfaces and Colloids·Maya SawadaYuji Goto

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