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Proteolysis-driven proliferation and rigidification of pepsin-resistant amyloid fibrils.
Cheong, Da Yeon; Roh, Seokbeom; Park, Insu; Lin, Yuxi; Lee, Young-Ho; Lee, Taeha; Lee, Sang Won; Lee, Dongtak; Jung, Hyo Gi; Kim, Hyunji; Lee, Wonseok; Yoon, Dae Sung; Hong, Yoochan; Lee, Gyudo.
Affiliation
  • Cheong DY; Department of Biotechnology and Bioinformatics, Korea University, Sejong 30019, South Korea; Interdisciplinary Graduate Program for Artificial Intelligence Smart Convergence Technology, Korea University, Sejong 30019, South Korea.
  • Roh S; Department of Biotechnology and Bioinformatics, Korea University, Sejong 30019, South Korea; Interdisciplinary Graduate Program for Artificial Intelligence Smart Convergence Technology, Korea University, Sejong 30019, South Korea.
  • Park I; Department of Biomedical Engineering, Konyang University, Daejeon 35365, South Korea.
  • Lin Y; Research Center for Bioconvergence Analysis, Korea Basic Science Institute, Ochang, Chungbuk 28119, South Korea.
  • Lee YH; Research Center for Bioconvergence Analysis, Korea Basic Science Institute, Ochang, Chungbuk 28119, South Korea; Bio-Analytical Science, University of Science and Technology, Daejeon 34113, South Korea; Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon 34134
  • Lee T; Department of Biotechnology and Bioinformatics, Korea University, Sejong 30019, South Korea; Interdisciplinary Graduate Program for Artificial Intelligence Smart Convergence Technology, Korea University, Sejong 30019, South Korea.
  • Lee SW; School of Biomedical Engineering, Korea University, Seoul 02841, South Korea.
  • Lee D; School of Biomedical Engineering, Korea University, Seoul 02841, South Korea.
  • Jung HG; School of Biomedical Engineering, Korea University, Seoul 02841, South Korea; Interdisciplinary Program in Precision Public Health, Korea University, Seoul 02841, South Korea.
  • Kim H; School of Biomedical Engineering, Korea University, Seoul 02841, South Korea; Interdisciplinary Program in Precision Public Health, Korea University, Seoul 02841, South Korea.
  • Lee W; Department of Electrical Engineering, Korea National University of Transportation, Chungju 27469, South Korea.
  • Yoon DS; School of Biomedical Engineering, Korea University, Seoul 02841, South Korea; Interdisciplinary Program in Precision Public Health, Korea University, Seoul 02841, South Korea; ASTRION Inc., Seoul 02841, South Korea. Electronic address: dsyoon@korea.ac.kr.
  • Hong Y; Department of Medical Devices, Korea Institute of Machinery and Materials (KIMM), Daegu 42994, South Korea. Electronic address: ychong1983@kimm.re.kr.
  • Lee G; Department of Biotechnology and Bioinformatics, Korea University, Sejong 30019, South Korea; Interdisciplinary Graduate Program for Artificial Intelligence Smart Convergence Technology, Korea University, Sejong 30019, South Korea. Electronic address: lkd0807@korea.ac.kr.
Int J Biol Macromol ; 227: 601-607, 2023 Feb 01.
Article in En | MEDLINE | ID: mdl-36543295
ABSTRACT
Proteolysis of amyloids is related to prevention and treatment of amyloidosis. What if the conditions for proteolysis were the same to those for amyloid formation? For example, pepsin, a gastric protease is activated in an acidic environment, which, interestingly, is also a condition that induces the amyloid formation. Here, we investigate the competition reactions between proteolysis and synthesis of amyloid under pepsin-activated conditions. The changes in the quantities and nanomechanical properties of amyloids after pepsin treatment were examined by fluorescence assay, circular dichroism and atomic force microscopy. We found that, in the case of pepsin-resistant amyloid, a secondary reaction can be accelerated, thereby proliferating amyloids. Moreover, after this reaction, the amyloid became 32.4 % thicker and 24.2 % stiffer than the original one. Our results suggest a new insight into the proteolysis-driven proliferation and rigidification of pepsin-resistant amyloids.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Pepsin A / Amyloid Language: En Journal: Int J Biol Macromol Year: 2023 Document type: Article Affiliation country: South Korea
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Pepsin A / Amyloid Language: En Journal: Int J Biol Macromol Year: 2023 Document type: Article Affiliation country: South Korea