Volume Constancy during Stretching of Spider Silk

2006 ◽  
Vol 7 (7) ◽  
pp. 2173-2177 ◽  
Author(s):  
G. V. Guinea ◽  
J. Pérez-Rigueiro ◽  
G. R. Plaza ◽  
M. Elices
Keyword(s):  
Spider Silk ◽  
Volume Constancy

Functional amyloid: widespread in Nature, diverse in purpose

2014 ◽  
Vol 56 ◽  
pp. 207-219 ◽  
Author(s):  
Chi L.L. Pham ◽  
Ann H. Kwan ◽  
Margaret Sunde
Keyword(s):  
Spider Silk ◽  
Epigenetic Inheritance ◽  
Fibrillar Structure ◽  
Cytoplasmic Polyadenylation ◽  
Functional Amyloid ◽  
Interacting Protein ◽  
Diverse Range ◽  
Element Binding Protein ◽  
Functional Amyloids ◽  
Micro Organisms

Amyloids are insoluble fibrillar protein deposits with an underlying cross-β structure initially discovered in the context of human diseases. However, it is now clear that the same fibrillar structure is used by many organisms, from bacteria to humans, in order to achieve a diverse range of biological functions. These functions include structure and protection (e.g. curli and chorion proteins, and insect and spider silk proteins), aiding interface transitions and cell–cell recognition (e.g. chaplins, rodlins and hydrophobins), protein control and storage (e.g. Microcin E492, modulins and PMEL), and epigenetic inheritance and memory [e.g. Sup35, Ure2p, HET-s and CPEB (cytoplasmic polyadenylation element-binding protein)]. As more examples of functional amyloid come to light, the list of roles associated with functional amyloids has continued to expand. More recently, amyloids have also been implicated in signal transduction [e.g. RIP1/RIP3 (receptor-interacting protein)] and perhaps in host defence [e.g. aDrs (anionic dermaseptin) peptide]. The present chapter discusses in detail functional amyloids that are used in Nature by micro-organisms, non-mammalian animals and mammals, including the biological roles that they play, their molecular composition and how they assemble, as well as the coping strategies that organisms have evolved to avoid the potential toxicity of functional amyloid.

Diversity of spider silk.

1998 ◽  
Vol 47 (2) ◽  
pp. 177-180 ◽  
Author(s):  
TOSHIYA MASUMOTO
Keyword(s):  
Spider Silk

High‐toughness Spider Silk Fibers Spun from Soluble Recombinant Silk Produced in Mammalian Cells

2003 ◽  
Author(s):  
Costas N. Karatzas ◽  
Nathalie Chretien ◽  
François Duguay ◽  
Annie Bellemare ◽  
Jiang Feng Zhou ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Spider Silk ◽  
Silk Fibers ◽  
High Toughness

scholarly journals Interfacial Crystallization and Supramolecular Self-Assembly of Spider Silk Inspired Protein at the Water-Air Interface

Materials ◽  
2021 ◽  
Vol 14 (15) ◽  
pp. 4239
Author(s):  
Pezhman Mohammadi ◽  
Fabian Zemke ◽  
Wolfgang Wagermaier ◽  
Markus B. Linder
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Assembly Process ◽  
Protein Solution ◽  
Time Resolved ◽  
Macromolecular Assembly ◽  
X Ray Scattering ◽  
Air Interface ◽  
Fundamental Research ◽  
Β Sheet

Macromolecular assembly into complex morphologies and architectural shapes is an area of fundamental research and technological innovation. In this work, we investigate the self-assembly process of recombinantly produced protein inspired by spider silk (spidroin). To elucidate the first steps of the assembly process, we examined highly concentrated and viscous pendant droplets of this protein in air. We show how the protein self-assembles and crystallizes at the water–air interface into a relatively thick and highly elastic skin. Using time-resolved in situ synchrotron X-ray scattering measurements during the drying process, we showed that the skin evolved to contain a high β-sheet amount over time. We also found that β-sheet formation strongly depended on protein concentration and relative humidity. These had a strong influence not only on the amount, but also on the ordering of these structures during the β-sheet formation process. We also showed how the skin around pendant droplets can serve as a reservoir for attaining liquid–liquid phase separation and coacervation from the dilute protein solution. Essentially, this study shows a new assembly route which could be optimized for the synthesis of new materials from a dilute protein solution and determine the properties of the final products.

scholarly journals Designing of spider silk proteins for hiPSC-based cardiac tissue engineering

2021 ◽  
pp. 100114
Author(s):  
Tilman U. Esser ◽  
Vanessa T. Trossmann ◽  
Sarah Lentz ◽  
Felix B. Engel ◽  
Thomas Scheibel
Keyword(s):  
Tissue Engineering ◽  
Spider Silk ◽  
Cardiac Tissue ◽  
Cardiac Tissue Engineering ◽  
Silk Proteins
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