Similarities in the Structural Organization of Major and Minor Ampullate Spider Silk

被引:37
作者
Papadopoulos, Periklis [1 ]
Ene, Roxana [1 ]
Weidner, Immanuel [1 ]
Kremer, Friedrich [1 ]
机构
[1] Univ Leipzig, Inst Expt Phys 1, D-04103 Leipzig, Germany
关键词
biomaterials; infrared spectroscopy; major ampullate; minor ampullate; spider silk; structure-property relations; FIBROIN GENE FAMILY; DRAGLINE SILK; VIBRATIONAL ANALYSIS; MECHANICAL-PROPERTIES; PROTEINS; POLYPEPTIDES; PEPTIDES; SEQUENCE; FIBER; BETA-POLY(L-ALANINE);
D O I
10.1002/marc.200900018
中图分类号
O63 [高分子化学(高聚物)];
学科分类号
070305 ; 080501 ; 081704 ;
摘要
Minor and major ampullate spider silks are studied under varying mechanical stress by static and time-resolved FT-IR spectroscopy. This enables one to trace the external mechanical excitation on a microscopic level and to determine for the different moieties the time dependence of the molecular order parameters and corresponding band shifts. It is concluded that the hierarchical nanostructure of both types of silk is similar, being composed of highly oriented nanocrystals, which are interconnected by amorphous chains that obey the worm-like chain model and have a Gaussian distribution of pre-strain. By that it is possible to describe the mechanical properties of both silks by two adjustable parameters only, the center and width of the distribution. For major ampullate silk, the observed variability is small in pronounced contrast to the findings for minor ampullate.
引用
收藏
页码:851 / 857
页数:7
相关论文
共 36 条
[1]   Silken toolkits:: biomechanics of silk fibers spun by the orb web spider Argiope argentata (Fabricius 1775) [J].
Blackledge, TA ;
Hayashi, CY .
JOURNAL OF EXPERIMENTAL BIOLOGY, 2006, 209 (13) :2452-2461
[2]   Spider minor ampullate silk proteins contain new repetitive sequences and highly conserved non-silk-like "spacer regions" [J].
Colgin, MA ;
Lewis, RV .
PROTEIN SCIENCE, 1998, 7 (03) :667-672
[3]   Secondary structures and conformational changes in flagelliform, cylindrical, major, and minor ampullate silk proteins. Temperature and concentration effects [J].
Dicko, C ;
Knight, D ;
Kenney, JM ;
Vollrath, F .
BIOMACROMOLECULES, 2004, 5 (06) :2105-2115
[4]   VIBRATIONAL ANALYSIS OF PEPTIDES, POLYPEPTIDES, AND PROTEINS .15. CRYSTALLINE POLYGLYCINE-II [J].
DWIVEDI, AM ;
KRIMM, S .
BIOPOLYMERS, 1982, 21 (12) :2377-2397
[5]   VIBRATIONAL ANALYSIS OF PEPTIDES, POLYPEPTIDES, AND PROTEINS .11. BETA-POLY(L-ALANINE) AND ITS N-DEUTERATED DERIVATIVE [J].
DWIVEDI, AM ;
KRIMM, S .
MACROMOLECULES, 1982, 15 (01) :186-193
[6]   VIBRATIONAL ANALYSIS OF PEPTIDES, POLYPEPTIDES, AND PROTEINS .10. POLY(GLYCINE-I) AND ITS ISOTOPIC DERIVATIVES [J].
DWIVEDI, AM ;
KRIMM, S .
MACROMOLECULES, 1982, 15 (01) :177-185
[7]   THE STRUCTURE AND PROPERTIES OF SPIDER SILK [J].
GOSLINE, JM ;
DEMONT, ME ;
DENNY, MW .
ENDEAVOUR, 1986, 10 (01) :37-43
[8]  
Gosline JM, 1999, J EXP BIOL, V202, P3295
[9]   Silk properties determined by gland-specific expression of a spider fibroin gene family [J].
Guerette, PA ;
Ginzinger, DG ;
Weber, BHF ;
Gosline, JM .
SCIENCE, 1996, 272 (5258) :112-115
[10]   Volume constancy during stretching of spider silk [J].
Guinea, G. V. ;
Perez-Rigueiro, J. ;
Plaza, G. R. ;
Elices, M. .
BIOMACROMOLECULES, 2006, 7 (07) :2173-2177