A comparison of the mechanical and structural properties of fibrin fibers with other protein fibers

被引:173
作者
Guthold, M. [1 ]
Liu, W.
Sparks, E. A.
Jawerth, L. M.
Peng, L.
Falvo, M.
Superfine, R.
Hantgan, R. R.
Lord, S. T.
机构
[1] Wake Forest Univ, Dept Phys, Winston Salem, NC 27109 USA
[2] Harvard Univ, Dept Phys, Cambridge, MA 02138 USA
[3] Univ N Carolina, Curriculum Appl & Mat Sci, Chapel Hill, NC 27599 USA
[4] Wake Forest Univ, Dept Biochem, Winston Salem, NC 27157 USA
[5] Univ N Carolina, Dept Pathol & Lab Med, Chapel Hill, NC 27599 USA
关键词
stiffness; young's modulus; breaking strain; rupture strain; extensibility; fibrin fiber; elastin; resilin; spider silk; fibrillin; fibronectin; myofibrils; intermediate filament; keratin; actin filament; microtubules; collagen; mussel byssus;
D O I
10.1007/s12013-007-9001-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In the past few years a great deal of progress has been made in studying the mechanical and structural properties of biological protein fibers. Here, we compare and review the stiffness (Young's modulus, E) and breaking strain (also called rupture strain or extensibility, epsilon(max)) of numerous biological protein fibers in light of the recently reported mechanical properties of fibrin fibers. Emphasis is also placed on the structural features and molecular mechanisms that endow biological protein fibers with their respective mechanical properties. Generally, stiff biological protein fibers have a Young's modulus on the order of a few Gigapascal and are not very extensible (epsilon(max) < 20%). They also display a very regular arrangement of their monomeric units. Soft biological protein fibers have a Young's modulus on the order of a few Megapascal and are very extensible (epsilon(max) > 100%). These soft, extensible fibers employ a variety of molecular mechanisms, such as extending amorphous regions or unfolding protein domains, to accommodate large strains. We conclude our review by proposing a novel model of how fibrin fibers might achieve their extremely large extensibility, despite the regular arrangement of the monomeric fibrin units within a fiber. We propose that fibrin fibers accommodate large strains by two major mechanisms: (1) an alpha-helix to ss-strand conversion of the coiled coils; (2) a partial unfolding of the globular C-terminal domain of the gamma-chain.
引用
收藏
页码:165 / 181
页数:17
相关论文
共 109 条
[11]   COAGULATION STUDIES ON REPTILASE, AN EXTRACT OF THE VENOM FROM BOTHROPS-JARARACA [J].
BLOMBACK, B ;
BLOMBACK, M ;
NILSSON, IM .
THROMBOSIS ET DIATHESIS HAEMORRHAGICA, 1957, 1 (01) :76-86
[12]  
BRAATEN JV, 1994, BLOOD, V83, P982
[13]   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
[14]   The crystal structure of modified bovine fibrinogen [J].
Brown, JH ;
Volkmann, N ;
Jun, G ;
Henschen-Edman, AH ;
Cohen, C .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (01) :85-90
[15]   Identification of an ordered compact structure within the recombinant bovine fibrinogen αC-domain fragment by NMRT [J].
Burton, RA ;
Tsurupa, G ;
Medved, L ;
Tjandra, N .
BIOCHEMISTRY, 2006, 45 (07) :2257-2266
[16]   Protofibrils within fibrin fibres are packed together in a regular array [J].
Caracciolo, G ;
De Spirito, M ;
Castellano, AC ;
Pozzi, D ;
Amiconi, G ;
De Pascalis, A ;
Caminiti, R ;
Arcovito, G .
THROMBOSIS AND HAEMOSTASIS, 2003, 89 (04) :632-636
[17]   SIZE AND DENSITY OF FIBRIN FIBERS FROM TURBIDITY [J].
CARR, ME ;
HERMANS, J .
MACROMOLECULES, 1978, 11 (01) :46-50
[18]  
CHEN R, 1971, BIOCHEMISTRY-US, V10, P15610
[19]   Why fibrous proteins are romantic [J].
Cohen, C .
JOURNAL OF STRUCTURAL BIOLOGY, 1998, 122 (1-2) :3-16
[20]   ULTRASTRUCTURE OF CLOTS DURING ISOMETRIC CONTRACTION [J].
COHEN, I ;
GERRARD, JM ;
WHITE, JG .
JOURNAL OF CELL BIOLOGY, 1982, 93 (03) :775-787