Aggregates with lysozyme and ovalbumin show features of amyloid-like fibrils

Yasushi Sugimoto, Yoshiki Kamada, Yuhei Tokunaga, Hiroshi Shinohara, Mitsuharu Matsumoto, Takahiro Kusakabe, Takatoshi Ohkuri, Tadashi Ueda

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

The interaction of egg-white lysozyme with N-ovalbumin, the native form of egg-white ovalbumin with the denaturation temperature, T m, of 78 °C, was investigated by the inhibition of lysozyme muramidase activity, differential scanning calorimetry, and circular dichroism assay as indicators. Signals for the interaction were the most prominent when the mixture of lysozyme and N-ovalbumin was co-heated at 72 °C, slightly lower than the T m of N-ovalbumin. The interaction was also marked when unheated lysozyme was mixed with N-ovalbumin preheated at 72 °C. Moreover, the mixture rapidly formed fibrous precipitates, which were positive for thioflavin T fluorescent emission, a marker for the amyloid fibril formation. Also electron microscopic observation exhibited features of fibrils. The interaction potency of ovalbumin was ascribed to the tryptic fragment ILELPFASGT MSMLVLLPDE VSGLEQLESIINFEK (residues 229-263), derived from the 2B strands 2 and 3 of ovalbumin. From lysozyme, on the other hand, the chymotryptic peptide RNRCKGTDVQAW (residues 112-123), including cluster 6, and the chymotryptic/tryptic peptide GILQINSRW (residues 54-62), including cluster 3, were responsible for the interaction with N-ovalbumin. Interestingly, this nonamer peptide was found to have the ability to self-aggregate. To the authors knowledge, this may be the first report to document the possible involvement of dual proteins in the formation of amyloid-like fibrils.

Original languageEnglish
Pages (from-to)533-544
Number of pages12
JournalBiochemistry and Cell Biology
Volume89
Issue number6
DOIs
Publication statusPublished - Dec 2011

Fingerprint

Ovalbumin
Muramidase
Amyloid
Egg White
Peptides
Denaturation
Differential Scanning Calorimetry
Circular Dichroism
Precipitates
Differential scanning calorimetry
Assays
Electrons
Temperature

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Aggregates with lysozyme and ovalbumin show features of amyloid-like fibrils. / Sugimoto, Yasushi; Kamada, Yoshiki; Tokunaga, Yuhei; Shinohara, Hiroshi; Matsumoto, Mitsuharu; Kusakabe, Takahiro; Ohkuri, Takatoshi; Ueda, Tadashi.

In: Biochemistry and Cell Biology, Vol. 89, No. 6, 12.2011, p. 533-544.

Research output: Contribution to journalArticle

Sugimoto, Y, Kamada, Y, Tokunaga, Y, Shinohara, H, Matsumoto, M, Kusakabe, T, Ohkuri, T & Ueda, T 2011, 'Aggregates with lysozyme and ovalbumin show features of amyloid-like fibrils', Biochemistry and Cell Biology, vol. 89, no. 6, pp. 533-544. https://doi.org/10.1139/o11-041
Sugimoto, Yasushi ; Kamada, Yoshiki ; Tokunaga, Yuhei ; Shinohara, Hiroshi ; Matsumoto, Mitsuharu ; Kusakabe, Takahiro ; Ohkuri, Takatoshi ; Ueda, Tadashi. / Aggregates with lysozyme and ovalbumin show features of amyloid-like fibrils. In: Biochemistry and Cell Biology. 2011 ; Vol. 89, No. 6. pp. 533-544.
@article{57be320089644c929ebb14cc5fec4478,
title = "Aggregates with lysozyme and ovalbumin show features of amyloid-like fibrils",
abstract = "The interaction of egg-white lysozyme with N-ovalbumin, the native form of egg-white ovalbumin with the denaturation temperature, T m, of 78 °C, was investigated by the inhibition of lysozyme muramidase activity, differential scanning calorimetry, and circular dichroism assay as indicators. Signals for the interaction were the most prominent when the mixture of lysozyme and N-ovalbumin was co-heated at 72 °C, slightly lower than the T m of N-ovalbumin. The interaction was also marked when unheated lysozyme was mixed with N-ovalbumin preheated at 72 °C. Moreover, the mixture rapidly formed fibrous precipitates, which were positive for thioflavin T fluorescent emission, a marker for the amyloid fibril formation. Also electron microscopic observation exhibited features of fibrils. The interaction potency of ovalbumin was ascribed to the tryptic fragment ILELPFASGT MSMLVLLPDE VSGLEQLESIINFEK (residues 229-263), derived from the 2B strands 2 and 3 of ovalbumin. From lysozyme, on the other hand, the chymotryptic peptide RNRCKGTDVQAW (residues 112-123), including cluster 6, and the chymotryptic/tryptic peptide GILQINSRW (residues 54-62), including cluster 3, were responsible for the interaction with N-ovalbumin. Interestingly, this nonamer peptide was found to have the ability to self-aggregate. To the authors knowledge, this may be the first report to document the possible involvement of dual proteins in the formation of amyloid-like fibrils.",
author = "Yasushi Sugimoto and Yoshiki Kamada and Yuhei Tokunaga and Hiroshi Shinohara and Mitsuharu Matsumoto and Takahiro Kusakabe and Takatoshi Ohkuri and Tadashi Ueda",
year = "2011",
month = "12",
doi = "10.1139/o11-041",
language = "English",
volume = "89",
pages = "533--544",
journal = "Biochemistry and Cell Biology",
issn = "0829-8211",
publisher = "National Research Council of Canada",
number = "6",

}

TY - JOUR

T1 - Aggregates with lysozyme and ovalbumin show features of amyloid-like fibrils

AU - Sugimoto, Yasushi

AU - Kamada, Yoshiki

AU - Tokunaga, Yuhei

AU - Shinohara, Hiroshi

AU - Matsumoto, Mitsuharu

AU - Kusakabe, Takahiro

AU - Ohkuri, Takatoshi

AU - Ueda, Tadashi

PY - 2011/12

Y1 - 2011/12

N2 - The interaction of egg-white lysozyme with N-ovalbumin, the native form of egg-white ovalbumin with the denaturation temperature, T m, of 78 °C, was investigated by the inhibition of lysozyme muramidase activity, differential scanning calorimetry, and circular dichroism assay as indicators. Signals for the interaction were the most prominent when the mixture of lysozyme and N-ovalbumin was co-heated at 72 °C, slightly lower than the T m of N-ovalbumin. The interaction was also marked when unheated lysozyme was mixed with N-ovalbumin preheated at 72 °C. Moreover, the mixture rapidly formed fibrous precipitates, which were positive for thioflavin T fluorescent emission, a marker for the amyloid fibril formation. Also electron microscopic observation exhibited features of fibrils. The interaction potency of ovalbumin was ascribed to the tryptic fragment ILELPFASGT MSMLVLLPDE VSGLEQLESIINFEK (residues 229-263), derived from the 2B strands 2 and 3 of ovalbumin. From lysozyme, on the other hand, the chymotryptic peptide RNRCKGTDVQAW (residues 112-123), including cluster 6, and the chymotryptic/tryptic peptide GILQINSRW (residues 54-62), including cluster 3, were responsible for the interaction with N-ovalbumin. Interestingly, this nonamer peptide was found to have the ability to self-aggregate. To the authors knowledge, this may be the first report to document the possible involvement of dual proteins in the formation of amyloid-like fibrils.

AB - The interaction of egg-white lysozyme with N-ovalbumin, the native form of egg-white ovalbumin with the denaturation temperature, T m, of 78 °C, was investigated by the inhibition of lysozyme muramidase activity, differential scanning calorimetry, and circular dichroism assay as indicators. Signals for the interaction were the most prominent when the mixture of lysozyme and N-ovalbumin was co-heated at 72 °C, slightly lower than the T m of N-ovalbumin. The interaction was also marked when unheated lysozyme was mixed with N-ovalbumin preheated at 72 °C. Moreover, the mixture rapidly formed fibrous precipitates, which were positive for thioflavin T fluorescent emission, a marker for the amyloid fibril formation. Also electron microscopic observation exhibited features of fibrils. The interaction potency of ovalbumin was ascribed to the tryptic fragment ILELPFASGT MSMLVLLPDE VSGLEQLESIINFEK (residues 229-263), derived from the 2B strands 2 and 3 of ovalbumin. From lysozyme, on the other hand, the chymotryptic peptide RNRCKGTDVQAW (residues 112-123), including cluster 6, and the chymotryptic/tryptic peptide GILQINSRW (residues 54-62), including cluster 3, were responsible for the interaction with N-ovalbumin. Interestingly, this nonamer peptide was found to have the ability to self-aggregate. To the authors knowledge, this may be the first report to document the possible involvement of dual proteins in the formation of amyloid-like fibrils.

UR - http://www.scopus.com/inward/record.url?scp=84857339663&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84857339663&partnerID=8YFLogxK

U2 - 10.1139/o11-041

DO - 10.1139/o11-041

M3 - Article

C2 - 22004604

AN - SCOPUS:84857339663

VL - 89

SP - 533

EP - 544

JO - Biochemistry and Cell Biology

JF - Biochemistry and Cell Biology

SN - 0829-8211

IS - 6

ER -