An engineered spider silk protein forms microspheres

被引：129
作者：
Slotta, Ute K. [1 ]
Rammensee, Sebastian [2 ]
Gorb, Stanislav [3 ]
Scheibel, Thomas [1 ]
机构：
[1] Tech Univ Munich, Lehrstuhl Biotechnol, Dept Chem, D-85747 Garching, Germany
[2] Tech Univ Munich, Lehrstuhl Biophys, Dept Phys, D-85747 Garching, Germany
[3] Max Planck Inst Met Res, Evolutionary Biomat Grp, D-70569 Stuttgart, Germany
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2008年 / 47卷 / 24期
关键词：
biomaterials; Hofmeister effect; nanostructures; phase separation; self-assembly;
D O I：
10.1002/anie.200800683
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
(Figure Presented) Fibrils or spheres? Spider silk proteins belong to the class of natively unfolded proteins. Depending on the experimental conditions, these proteins form nanofibrils or microspheres following two distinct aggregation pathways. A detailed model describes the assembly mechanism of spider silk proteins into microspheres. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码：4592 / 4594
页数：3
相关论文
共 18 条
  • [1] Hierarchical organization in aggregates of protein molecules
    Bohr, H
    Kuhle, A
    Sorensen, AH
    Bohr, J
    [J]. ZEITSCHRIFT FUR PHYSIK D-ATOMS MOLECULES AND CLUSTERS, 1997, 40 (1-4): : 513 - 515
  • [2] Exler J. H., 2007, ANGEW CHEM, V119, P3629
  • [3] The amphiphilic properties of spider silks are important for spinning
    Exler, Josef H.
    Huemmerich, Daniel
    Scheibel, Thomas
    [J]. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2007, 46 (19) : 3559 - 3562
  • [4] Ultrastructure of insect and spider cocoon silks
    Hakimi, Osnat
    Knight, David P.
    Knight, Martin M.
    Grahn, Michael F.
    Vadgama, Pankaj
    [J]. BIOMACROMOLECULES, 2006, 7 (10) : 2901 - 2908
  • [5] Hofmeister F., 1888, Arch. Exp. Pathol. Pharmakol, V24, P247, DOI DOI 10.1007/BF01918191
  • [6] Processing and modification of films made from recombinant spider silk proteins
    Huemmerich, D
    Slotta, U
    Scheibel, T
    [J]. APPLIED PHYSICS A-MATERIALS SCIENCE & PROCESSING, 2006, 82 (02): : 219 - 222
  • [7] Novel assembly properties of recombinant spider dragline silk proteins
    Huemmerich, D
    Scheibel, T
    Vollrath, F
    Cohen, S
    Gat, U
    Ittah, S
    [J]. CURRENT BIOLOGY, 2004, 14 (22) : 2070 - 2074
  • [8] Primary structure elements of spider dragline silks and their contribution to protein solubility
    Huemmerich, D
    Helsen, CW
    Quedzuweit, S
    Oschmann, J
    Rudolph, R
    Scheibel, T
    [J]. BIOCHEMISTRY, 2004, 43 (42) : 13604 - 13612
  • [9] Amyloidogenic nature of spider silk
    Kenney, JM
    Knight, D
    Wise, MJ
    Vollrath, F
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 2002, 269 (16): : 4159 - 4163
  • [10] Salt-induced protein precipitation in aqueous solution: Single and binary protein systems
    Kim, SG
    Bae, YC
    [J]. MACROMOLECULAR RESEARCH, 2003, 11 (01) : 53 - 61
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