TY - JOUR
T1 - Proteolysis-driven proliferation and rigidification of pepsin-resistant amyloid fibrils
AU - Cheong, Da Yeon
AU - Roh, Seokbeom
AU - Park, Insu
AU - Lin, Yuxi
AU - Lee, Young Ho
AU - Lee, Taeha
AU - Lee, Sang Won
AU - Lee, Dongtak
AU - Jung, Hyo Gi
AU - Kim, Hyunji
AU - Lee, Wonseok
AU - Yoon, Dae Sung
AU - Hong, Yoochan
AU - Lee, Gyudo
N1 - Publisher Copyright:
© 2022
PY - 2023/2/1
Y1 - 2023/2/1
N2 - 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.
AB - 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.
KW - Amyloid proliferation
KW - Amyloid stiffening
KW - Atomic force microscopy
KW - Pepsin
KW - Proteolysis of amyloid
UR - http://www.scopus.com/inward/record.url?scp=85144581792&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2022.12.104
DO - 10.1016/j.ijbiomac.2022.12.104
M3 - Article
C2 - 36543295
AN - SCOPUS:85144581792
SN - 0141-8130
VL - 227
SP - 601
EP - 607
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -