期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 111, 期 27, 页码 E2780-E2786出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1402909111
关键词
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资金
- National Science Foundation (NSF) [Civil, Mechanical, and Manufacturing Innovation (CMMI)] [1100339]
- NSF (CMMI) [0954825, 1100791]
- National Institutes of Health [R01HL 098028]
- NSF (GK12) [0840889]
- MD Anderson Professorship
- National Natural Science Foundation (NSFC) [11325420]
- Project 973 [2014CB848800]
- Dengfeng Project B of Nanjing University
- NSFC [U1332205]
- Directorate For Engineering
- Div Of Civil, Mechanical, & Manufact Inn [1100791] Funding Source: National Science Foundation
- Div Of Civil, Mechanical, & Manufact Inn
- Directorate For Engineering [1100339, 0954825] Funding Source: National Science Foundation
Ferroelectricity has long been speculated to have important biological functions, although its very existence in biology has never been firmly established. Here, we present compelling evidence that elastin, the key ECM protein found in connective tissues, is ferroelectric, and we elucidate the molecular mechanism of its switching. Nanoscale piezoresponse force microscopy and macroscopic pyroelectric measurements both show that elastin retains ferroelectricity at 473 K, with polarization on the order of 1 mu C/cm(2), whereas coarse-grained molecular dynamics simulations predict similar polarization with a Curie temperature of 580 K, which is higher than most synthetic molecular ferroelectrics. The polarization of elastin is found to be intrinsic in tropoelastin at the monomer level, analogous to the unit cell level polarization in classical perovskite ferroelectrics, and it switches via thermally activated cooperative rotation of dipoles. Our study sheds light onto a long-standing question on ferroelectric switching in biology and establishes ferroelectricity as an important biophysical property of proteins. This is a critical first step toward resolving its physiological significance and pathological implications.
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