scholarly journals Spider dragline silk as torsional actuator driven by humidity

2019 ◽  
Vol 5 (3) ◽  
pp. eaau9183 ◽  
Author(s):  
Dabiao Liu ◽  
Anna Tarakanova ◽  
Claire C. Hsu ◽  
Miao Yu ◽  
Shimin Zheng ◽  
...  
Keyword(s):  
Relative Humidity ◽  
Practical Interest ◽  
Artificial Muscles ◽  
Torsional Deformation ◽  
Dragline Silk ◽  
Spider Species ◽  
Spider Dragline Silk ◽  
Self Powered ◽  
Novel Design ◽  
Torsional Property

Self-powered actuation driven by ambient humidity is of practical interest for applications such as hygroscopic artificial muscles. We demonstrate that spider dragline silk exhibits a humidity-induced torsional deformation of more than 300°/mm. When the relative humidity reaches a threshold of about 70%, the dragline silk starts to generate a large twist deformation independent of spider species. The torsional actuation can be precisely controlled by regulating the relative humidity. The behavior of humidity-induced twist is related to the supercontraction behavior of spider dragline silk. Specifically, molecular simulations of MaSp1 and MaSp2 proteins in dragline silk reveal that the unique torsional property originates from the presence of proline in MaSp2. The large proline rings also contribute to steric exclusion and disruption of hydrogen bonding in the molecule. This property of dragline silk and its structural origin can inspire novel design of torsional actuators or artificial muscles and enable the development of designer biomaterials.

SPIDER DRAGLINE SILK: CORRELATED AND MOSAIC EVOLUTION IN HIGH-PERFORMANCE BIOLOGICAL MATERIALS

Evolution ◽  
2006 ◽  
Vol 60 (12) ◽  
pp. 2539 ◽  
Author(s):  
Brook O. Swanson ◽  
Todd A. Blackledge ◽  
Adam P. Summers ◽  
Cheryl Y. Hayashi
Keyword(s):  
High Performance ◽  
Biological Materials ◽  
Dragline Silk ◽  
Spider Dragline Silk ◽  
Mosaic Evolution

Programmable Contractile Actuations of Twisted Spider Dragline Silk Yarns

2021 ◽  
Author(s):  
Lizhong Dong ◽  
Jian Qiao ◽  
Yulong Wu ◽  
Ming Ren ◽  
Yulian Wang ◽  
...  
Keyword(s):  
Dragline Silk ◽  
Spider Dragline Silk

Spider Dragline Silk

1999 ◽  
Vol 39 (4) ◽  
pp. 643-653 ◽  
Author(s):  
STEVEN B. WARNER ◽  
MALCOLM POLK ◽  
KARL JACOB
Keyword(s):  
Dragline Silk ◽  
Spider Dragline Silk

Supercontraction in Nephila spider dragline silk – Relaxation into equilibrium state

Polymer ◽  
2011 ◽  
Vol 52 (26) ◽  
pp. 6056-6060 ◽  
Author(s):  
Roxana Ene ◽  
Periklis Papadopoulos ◽  
Friedrich Kremer
Keyword(s):  
Equilibrium State ◽  
Dragline Silk ◽  
Spider Dragline Silk

Artificial spider silk is smart like natural one: having humidity-sensitive shape memory with superior recovery stress

2019 ◽  
Vol 3 (11) ◽  
pp. 2472-2482 ◽  
Author(s):  
Harun Venkatesan ◽  
Jianming Chen ◽  
Haiyang Liu ◽  
Yoonjung Kim ◽  
Sungsoo Na ◽  
...  
Keyword(s):  
Shape Memory ◽  
Spider Silk ◽  
Recovery Stress ◽  
Dragline Silk ◽  
Spider Dragline Silk ◽  
Shape Memory Behaviour

Inspired by supercontraction, the recombinant spider dragline silk displayed humidity-responsive shape memory behaviour with impressive recovery stress.

Raman Spectroscopic Evidence for Side-Chain Unfolding in Spider Dragline Silk under Tensile Deformation

2005 ◽  
Vol 874 ◽  
Author(s):  
Xiaojun He ◽  
Michael S. Ellison ◽  
Jacqueline M. Palmer
Keyword(s):  
Structural Changes ◽  
Tensile Deformation ◽  
Raman Band ◽  
Side Chain ◽  
Dragline Silk ◽  
Spider Dragline Silk ◽  
Raman Spectroscopic ◽  
Lateral Coupling ◽  
Silk Peptide ◽  
Random Configuration

AbstractIn-situ Ramanspectra were collected on the N. clavipes spider dragline silk under a tensile deformation rate of 15mm/min. The most prominent features on the spectra were due to those bands near 1100 cm-1, which present as a sensitive probe to structural changes associated with side-chains of silk peptide. A downshift of Raman bands at 1095 cm-1 and 1089 cm-1 was detected with increasing strain. Furthermore, an increase in the intensity of the Raman band at 1062 cm-1 due to the vibration of trans structure without lateral coupling was prominent at certain strain levels. This was interpreted in terms of a morphology transition from the random configuration to the trans conformation modulated by the reorganization of the hydrogen bonding among the side-chain.

Triggered Morphology Generation in a Biosynthetic Model Spider Dragline Silk Protein

1999 ◽  
Vol 5 (S2) ◽  
pp. 1214-1215
Author(s):  
R. Valluzzi ◽  
S. Szela ◽  
D. Kirschner ◽  
D. Kaplan
Keyword(s):  
Recombinant Dna ◽  
Consensus Sequence ◽  
Water Soluble ◽  
Nephila Clavipes ◽  
Dragline Silk ◽  
Spider Dragline Silk ◽  
Structure Changes ◽  
Methionine Residues ◽  
Recombinant Dna Techniques ◽  
Β Sheet

Recombinant DNA techniques were used to prepare a protein modeled after the consensus sequence of Nephila clavipesspider dragline silk, incorporating methionine residues to serve as redox “triggers”. In addition a water-soluble 27 residue peptide model of the dragline silk consensus amorphous sequence, representing a single amorphous block in the protein sequence, was prepared and characterized to gain additional insight into the behavior of the amorphous phase. X-ray diffraction, electron diffraction, transmission electron microscopy (TEM), and Fourier transform infrared spectroscopy (FTIR) were used to characterize the ability of the recombinant protein to form (β-sheet crystals and the effect of the oxidation state of the redox trigger on crystallinity and noncrystalline order in the sample. The formation of intractable β-sheet crystallites is a major cause of insolubility in proteins that can form this type of secondary structure. Changes in crystallinity were observed when triggered/reduced (insoluble) and untriggered/oxidized (soluble) protein samples were compared.

Sign in / Sign up

Export Citation Format

Share Document