Ferroelectric switching of elastin.

Abstract:

: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 μC/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.

authors

Liu Y,Cai HL,Zelisko M,Wang Y,Sun J,Yan F,Ma F,Wang P,Chen QN,Zheng H,Meng X,Sharma P,Zhang Y,Li J

doi

10.1073/pnas.1402909111

subject

Has Abstract

pub_date

2014-07-08 00:00:00

pages

E2780-6

issue

27

eissn

0027-8424

issn

1091-6490

pii

1402909111

journal_volume

111

pub_type

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