Download Physicists Identify Factors Governing Protein Aggregation, a

Physicists Identify Factors Governing Protein Aggregation, a Hallmark of
Neurodegenerative Diseases
2011-01-11 10:46:22
Dr. Chin-Kun Hu, a Research Fellow at Laboratory of Statistical and Computational
Physics of the Institute of Physics at Academia Sinica, and his collaborators have recently
identified a number of key factors governing protein aggregation. Increasing understanding
of protein aggregation is important as protein aggregation is thought to play an important
role in the onset and progression of neurodegenerative diseases such as Alzheimer’s
disease and Parkinson’s disease. The group’s results have been published in a series of
papers in Physical Review Letters (PRL) and Journal of the Physical Society of Japan
(JPSJ).
Neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, Huntington's
disease, spinocerebellar atrophy and frontotemporal lobar degeneration are caused by
progressive loss of structure and function of neurons (including death of neurons) due to
protein aggregation. For example, Alzheimer's disease is thought to be related to the
aggregation of Aβ 40 (a protein made up of 40 amino acids) and Aβ 42 (a protein made
up of 42 amino acids), while Huntington's disease and spinocerebellar atrophy are related
to aggregation of PolyQ (a protein with a long sequence of the amino acid glutamine).
In a study published in Physical Review Letters on 19 November, 2010, Dr. Chin-Kun Hu
and his collaborators based in Poland, Vietnam and the US, used a lattice model to study
the aggregation rates of proteins. They found that the probability of a protein sequence
appearing in an aggregated conformation can be used to determine the temperature at
which the protein can aggregate most easily. They also found a correlation between the
time taken for the protein to aggregate and the strength of interactions between charged
amino acids, which is consistent with previous experimental observations.
In another four articles published in the Journal of the Physical Society of Japan in
February, May and October 2010, Dr. Hu, together with Dr. Wen-Jong Ma (now a member
of the faculty at the Graduate Institute of Applied Physics, National Chengchi University,
Taiwan), employed molecular dynamics to study relaxation and aggregation of protein
chains under various conditions. They found that when the bending-angle dependent and
torsion-angle dependent interactions are zero or very small, the protein chains tend to
aggregate at lower temperatures. This finding has contributed to understanding the
aggregation of Aβ 40 and Aβ 42 in Alzheimer's disease.
As the next step of the project, Dr. Hu said that he and his collaborators would like to
combine the results from computer simulations and analytic calculations with experimental
data in an effort to formulate a general theory of protein aggregation to enable prediction
of the influence of environment, mutation and drugs on protein aggregation rates and also
predict the conditions most likely to prohibit protein aggregation.
The article published in Physical Review Letters entitled “Factors Governing
Fibrillogenesis of Polypeptide Chains Revealed by Lattice Models” is available at the
journal’s website at: http://prl.aps.org/abstract/PRL/v105/i21/e218101. The full list of
authors is: Mai Suan Li, Nguyen Truong Co, Govardhan Reddy, Chin-Kun Hu, J. E. Straub,
and D. Thirumalai. The other four articles are available at the website of the Journal of the
Physical Society of Japan (JPSJ) at: http://jpsj.ipap.jp/
Related websites:
Laboratory of Statistical and Computational Physics: http://proj1.sinica.edu.tw/~statphys
Media contacts:
Dr. Chin-Kun Hu, Institute of Physics, Academia Sinica
(Tel) +886-2-2789-6720
Fang-Hsun Yeh, Office of Public Affairs, Central Office of Administration, Academia
Sinica (Tel) +886-2-2789-8820, (Fax) +886-2-2782-1551, (M) 0922-036-691
E-mail: [email protected]
Mei-Hui Lin, Office of Public Affairs, Central Office of Administration, Academia Sinica
(Tel) +886-2-2789-8821, (Fax) +886-2-2782-1551, (M) 0921-845-234
E-mail: [email protected]
Release Unit : Office of Public Affairs
最後更新：中華民國 100 年 01 月 11 日