Deformation and failure of protein materials in physiologically extreme conditions and disease

被引:274
作者
Buehler, Markus J. [1 ,2 ,3 ]
Yung, Yu Ching [4 ]
机构
[1] MIT, Dept Civil & Environm Engn, Lab Atomist & Mol Mech, Cambridge, MA 02139 USA
[2] MIT, Ctr Computat Engn, Cambridge, MA 02139 USA
[3] MIT, Ctr Mat Sci & Engn, Cambridge, MA 02139 USA
[4] Harvard Univ, Sch Engn & Appl Sci, Lab Cell & Tissue Engn, Cambridge, MA 02138 USA
基金
美国国家科学基金会;
关键词
MOLECULAR-DYNAMICS SIMULATIONS; OSTEOGENESIS IMPERFECTA; INTERMEDIATE-FILAMENTS; MECHANICAL-PROPERTIES; NUCLEAR LAMINA; BIOMECHANICAL PROPERTIES; ASSEMBLY MECHANISM; ALZHEIMERS-DISEASE; COLLAGEN FIBRILS; FORCE-FIELDS;
D O I
10.1038/nmat2387
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070305 [高分子化学与物理];
摘要
Biological protein materials feature hierarchical structures that make up a diverse range of physiological materials. The analysis of protein materials is an emerging field that uses the relationships between biological structures, processes and properties to probe deformation and failure phenomena at the molecular and microscopic level. Here we discuss how advanced experimental, computational and theoretical methods can be used to assess structure-process-property relations and to monitor and predict mechanisms associated with failure of protein materials. Case studies are presented to examine failure phenomena in the progression of disease. From this materials science perspective, a de novo basis for understanding biological processes can be used to develop new approaches for treating medical disorders. We highlight opportunities to use knowledge gained from the integration of multiple scales with physical, biological and chemical concepts for potential applications in materials design and nanotechnology.
引用
收藏
页码:175 / 188
页数:14
相关论文
共 141 条
[1]
Brainstorming tumors and nanomedicine: The 2nd Annual Cancer Nanobiology Think Tank [J].
Dimitrov, Dimiter S. .
JOURNAL OF COMPUTATIONAL AND THEORETICAL NANOSCIENCE, 2008, 5 (01) :1-6
[2]
Hierarchies, multiple energy barriers, and robustness govern the fracture mechanics of α-helical and β-sheet protein domains [J].
Ackbarow, Theodor ;
Chen, Xuefeng ;
Keten, Sinan ;
Buehler, Markus J. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (42) :16410-16415
[3]
THE NUCLEAR LAMINA IS A MESHWORK OF INTERMEDIATE-TYPE FILAMENTS [J].
AEBI, U ;
COHN, J ;
BUHLE, L ;
GERACE, L .
NATURE, 1986, 323 (6088) :560-564
[4]
Alberts B., 2007, Molecular Biology of the Cell. (4th edition), Vfifth
[5]
Simplicity in biology [J].
Alon, Uri .
NATURE, 2007, 446 (7135) :497-497
[6]
Astbury WT., 1931, GEN PHILOS T R SOC L, V230, P75
[7]
BELL GI, 1978, SCIENCE, V200, P618, DOI 10.1126/science.347575
[8]
PROTEIN DATA BANK - COMPUTER-BASED ARCHIVAL FILE FOR MACROMOLECULAR STRUCTURES [J].
BERNSTEIN, FC ;
KOETZLE, TF ;
WILLIAMS, GJB ;
MEYER, EF ;
BRICE, MD ;
RODGERS, JR ;
KENNARD, O ;
SHIMANOUCHI, T ;
TASUMI, M .
JOURNAL OF MOLECULAR BIOLOGY, 1977, 112 (03) :535-542
[9]
Mapping domain structures in silks from insects and spiders related to protein assembly [J].
Bini, E ;
Knight, DP ;
Kaplan, DL .
JOURNAL OF MOLECULAR BIOLOGY, 2004, 335 (01) :27-40
[10]
Forced unfolding of coiled-coils in fibrinogen by single-molecule AFM [J].
Brown, Andre E. X. ;
Litvinov, Rustem I. ;
Discher, Dennis E. ;
Weisel, John W. .
BIOPHYSICAL JOURNAL, 2007, 92 (05) :L39-L41