TY - GEN
T1 - Structural analysis of F20L oligomeric and protofibrillar amyloid pair structures using molecular dynamics simulations
AU - Chang, Hyun Joon
AU - Lee, Myeongsang
AU - Baek, Inchul
AU - Kim, Yoonjung
AU - Na, Sungsoo
N1 - Funding Information:
S. Na gratefully acknowledges funding from the Basic Science Research Program of the National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT & Future Planning (MSIP) (No. 2014R1A2A1A11052389). H. J. Chang is grateful for financial support from the Global Ph.D. Fellowship Program through the National Research Foundation of Korea (NRF), funded by the Ministry of Education (No. 2014H1A2A1021042).
Publisher Copyright:
© 2016 IEEE.
PY - 2016/12/7
Y1 - 2016/12/7
N2 - Ap amyloid protein is representative agent, which is involved in neuro-degenerative diseases. Due to the undegrading characteristics under physiological conditions, understanding the structural characteristics of Aβ amyloid protein in detail is crucial. Many efforts have made on the lowering the structural stabilities of Aβ amyloid protein by decreasing the aromatic residues characteristic and hydrophobic effect. However, there lacks an understanding of Aβ amyloid pair structures in detail. In this work, we provide the structural characteristics of Aβ amyloid pair structures by selective leucine residue mutation on phenylalanine residue (F20L). We also considered the polymorphic feature of F20L Aβ amyloid pair based on NN, CC and NC compositions. Furthermore, we found the structural difference of oligomeric and fibrillar NC F20L Aβ amyloid pair structures in detail.
AB - Ap amyloid protein is representative agent, which is involved in neuro-degenerative diseases. Due to the undegrading characteristics under physiological conditions, understanding the structural characteristics of Aβ amyloid protein in detail is crucial. Many efforts have made on the lowering the structural stabilities of Aβ amyloid protein by decreasing the aromatic residues characteristic and hydrophobic effect. However, there lacks an understanding of Aβ amyloid pair structures in detail. In this work, we provide the structural characteristics of Aβ amyloid pair structures by selective leucine residue mutation on phenylalanine residue (F20L). We also considered the polymorphic feature of F20L Aβ amyloid pair based on NN, CC and NC compositions. Furthermore, we found the structural difference of oligomeric and fibrillar NC F20L Aβ amyloid pair structures in detail.
UR - http://www.scopus.com/inward/record.url?scp=85010461759&partnerID=8YFLogxK
U2 - 10.1109/NMDC.2016.7777124
DO - 10.1109/NMDC.2016.7777124
M3 - Conference contribution
AN - SCOPUS:85010461759
T3 - Nanotechnology Materials and Devices Conference, NMDC 2016 - Conference Proceedings
BT - Nanotechnology Materials and Devices Conference, NMDC 2016 - Conference Proceedings
PB - Institute of Electrical and Electronics Engineers Inc.
T2 - 11th IEEE Nanotechnology Materials and Devices Conference, NMDC 2016
Y2 - 9 October 2016 through 12 October 2016
ER -