Tubuliform silk protein: A protein with unique molecular characteristics and mechanical properties in the spider silk fibroin family

2005 ◽  
Vol 82 (2) ◽  
pp. 265-273 ◽  
Author(s):  
M. Tian ◽  
R.V. Lewis
Keyword(s):  
Mechanical Properties ◽  
Silk Fibroin ◽  
Spider Silk ◽  
Protein A ◽  
Silk Protein ◽  
Molecular Characteristics

scholarly journals Presence of β-Turn Structure in Recombinant Spider Silk Dissolved in Formic Acid Revealed with NMR

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 511
Author(s):  
Yu Suzuki ◽  
Takanori Higashi ◽  
Takahiro Yamamoto ◽  
Hideyasu Okamura ◽  
Takehiro K. Sato ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Formic Acid ◽  
Spider Silk ◽  
Chemical Shifts ◽  
Repetitive Sequences ◽  
Silk Protein ◽  
Random Coil ◽  
Oh Groups ◽  
Spider Silk Protein ◽  
Turn Structure

Spider dragline silk is a biopolymer with excellent mechanical properties. The development of recombinant spider silk protein (RSP)-based materials with these properties is desirable. Formic acid (FA) is a spinning solvent for regenerated Bombyx mori silk fiber with excellent mechanical properties. To use FA as a spinning solvent for RSP with the sequence of major ampullate spider silk protein from Araneus diadematus, we determined the conformation of RSP in FA using solution NMR to determine the role of FA as a spinning solvent. We assigned 1H, 13C, and 15N chemical shifts to 32-residue repetitive sequences, including polyAla and Gly-rich regions of RSP. Chemical shift evaluation revealed that RSP is in mainly random coil conformation with partially type II β-turn structure in the Gly-Pro-Gly-X motifs of the Gly-rich region in FA, which was confirmed by the 15N NOE data. In addition, formylation at the Ser OH groups occurred in FA. Furthermore, we evaluated the conformation of the as-cast film of RSP dissolved in FA using solid-state NMR and found that β-sheet structure was predominantly formed.

Expression and Purification of a Spider Silk Protein: A New Strategy for Producing Repetitive Proteins

1996 ◽  
Vol 7 (4) ◽  
pp. 400-406 ◽  
Author(s):  
Randolph V. Lewis ◽  
Michael Hinman ◽  
Srinivas Kothakota ◽  
Maurille J. Fournier
Keyword(s):  
Spider Silk ◽  
Protein A ◽  
Silk Protein ◽  
Expression And Purification ◽  
New Strategy ◽  
Spider Silk Protein

scholarly journals Fabrication of flexible conductive silk fibroin/polythiophene membrane and its properties

e-Polymers ◽  
2021 ◽  
Vol 22 (1) ◽  
pp. 48-57
Author(s):  
Xin Ai ◽  
Shuqing Lu ◽  
Ailing Xie ◽  
Haoran Zhang ◽  
Juntao Zhao ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Electrical Conductivity ◽  
Hydroxyl Radical ◽  
Silk Fibroin ◽  
Silk Protein ◽  
Protein Film ◽  
Insulating Material ◽  
Conductive Material ◽  
Pedot Film ◽  
Silk Film

Abstract Silk fibroin (SF) film is an insulating material, which can be combined with polythiophene derivatives with electrical conductivity to obtain a flexible conductive material. In this work, poly(3,4-ethylenedioxythiophene) (PEDOT) was used to graft a silk protein film. The hydroxyl radical is formed by activation and oxidation of the silk protein film polymerized with the PEDOT radical formed by oxidation of 3,4-ethylenedioxythiophene to obtain a conductive silk film. The SF/PEDOT film, when tested, showed excellent electrical conductivity with resistance up to 63 Ω·cm−2, good flexibility, mechanical properties, fastness, and biocompatibility.

Mechanical Properties of Spider Silk for Use As a Biomaterial: Molecular Dynamics Investigations

2020 ◽  
Author(s):  
Atul Rawal ◽  
Kristen L. Rhinehardt ◽  
Ram V. Mohan
Keyword(s):  
Mechanical Properties ◽  
Molecular Dynamics ◽  
Spider Silk ◽  
Complete Separation ◽  
Silk Protein ◽  
Silk Proteins ◽  
Silk Fibers ◽  
Spider Silk Protein ◽  
Β Chain ◽  
Smd Simulations

Abstract Even though silkworm are the most dominant type of silk fibers used for commercial applications, spider silk has a definitive role in biomedical applications due to its biocompatibility and excellent mechanical properties as biomaterials. In recent years, recombinant production of the silk proteins at a larger scale has found new interest. Spider silk composites with a combination of a variety of other biomaterials have also been used to improve properties such as bio-compatibility, mechanical strength and controlled degradation. [1] A major constituent of spider silk fibers, are spidroin proteins. These are made up of repetitive segments flanked by conserved non-repetitive domains. The fiber proteins consist of a light chain and a heavy chain that are connected via a single disulfide bond. [2] Present paper employed steered molecular dynamics (SMD) as the principal method of investigating the mechanical properties of these nanoscale spider silk protein 3LR2, with a residual count of 134 amino acids. [3]. SMD simulations were performed by pulling on β-chain of the protein in the x-direction, while holding the other fixed. The focus of this paper is to investigate the mechanical properties of the nanoscale spider silk proteins with lengths of about 4.5nm in a folded state, leading to understanding of their feasibility in bio-printing of a composite spider silk biomaterial with a blend of various other biomaterials such as collagen. An in-depth insight into the fraying and tensile deformation and structural properties of the spider silk proteins are of innovative significance for a multitude of biomedical engineering applications. A calculated Gibbs free energy value of 18.59 kCal/mol via umbrella sampling corresponds with a complete separation of a single chain from a spider silk protein in case of fraying. Force needed for complete separation of the chain from the spider silk protein is analyzed, and discussed in this paper. It is found that the protein molecule undergoes a tensile stretch at strain rates of ≅ 11.65. An elastic modulus of 20.136 GPa, calculated via simple SMD simulations by subjecting the silk β-chain to a tensile stretch is also presented.

scholarly journals Anti-Inflammatory Properties of Injectable Betamethasone-Loaded Tyramine-Modified Gellan Gum/Silk Fibroin Hydrogels

Biomolecules ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 1456
Author(s):  
Isabel Matos Oliveira ◽  
Cristiana Gonçalves ◽  
Myeong Eun Shin ◽  
Sumi Lee ◽  
Rui Luis Reis ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Mechanical Properties ◽  
Silk Fibroin ◽  
Therapeutic Efficacy ◽  
Composite Structures ◽  
Gelation Time ◽  
Polymeric Materials ◽  
Gellan Gum ◽  
Traditional Use

Rheumatoid arthritis is a rheumatic disease for which a healing treatment does not presently exist. Silk fibroin has been extensively studied for use in drug delivery systems due to its uniqueness, versatility and strong clinical track record in medicine. However, in general, natural polymeric materials are not mechanically stable enough, and have high rates of biodegradation. Thus, synthetic materials such as gellan gum can be used to produce composite structures with biological signals to promote tissue-specific interactions while providing the desired mechanical properties. In this work, we aimed to produce hydrogels of tyramine-modified gellan gum with silk fibroin (Ty–GG/SF) via horseradish peroxidase (HRP), with encapsulated betamethasone, to improve the biocompatibility and mechanical properties, and further increase therapeutic efficacy to treat rheumatoid arthritis (RA). The Ty–GG/SF hydrogels presented a β-sheet secondary structure, with gelation time around 2–5 min, good resistance to enzymatic degradation, a suitable injectability profile, viscoelastic capacity with a significant solid component and a betamethasone-controlled release profile over time. In vitro studies showed that Ty–GG/SF hydrogels did not produce a deleterious effect on cellular metabolic activity, morphology or proliferation. Furthermore, Ty–GG/SF hydrogels with encapsulated betamethasone revealed greater therapeutic efficacy than the drug applied alone. Therefore, this strategy can provide an improvement in therapeutic efficacy when compared to the traditional use of drugs for the treatment of rheumatoid arthritis.

scholarly journals Is Dialdehyde Chitosan a Good Substance to Modify Physicochemical Properties of Biopolymeric Materials?

2021 ◽  
Vol 22 (7) ◽  
pp. 3391
Author(s):  
Sylwia Grabska-Zielińska ◽  
Alina Sionkowska ◽  
Ewa Olewnik-Kruszkowska ◽  
Katarzyna Reczyńska ◽  
Elżbieta Pamuła
Keyword(s):  
Mechanical Properties ◽  
Tissue Engineering ◽  
Physicochemical Properties ◽  
Silk Fibroin ◽  
Three Dimensional ◽  
Microscopy Imaging ◽  
Maximum Deformation ◽  
One Step ◽  
Chitosan Blends ◽  
Fourier Transfer Infrared Spectroscopy

The aim of this work was to compare physicochemical properties of three dimensional scaffolds based on silk fibroin, collagen and chitosan blends, cross-linked with dialdehyde starch (DAS) and dialdehyde chitosan (DAC). DAS was commercially available, while DAC was obtained by one-step synthesis. Structure and physicochemical properties of the materials were characterized using Fourier transfer infrared spectroscopy with attenuated total reflectance device (FTIR-ATR), swelling behavior and water content measurements, porosity and density observations, scanning electron microscopy imaging (SEM), mechanical properties evaluation and thermogravimetric analysis. Metabolic activity with AlamarBlue assay and live/dead fluorescence staining were performed to evaluate the cytocompatibility of the obtained materials with MG-63 osteoblast-like cells. The results showed that the properties of the scaffolds based on silk fibroin, collagen and chitosan can be modified by chemical cross-linking with DAS and DAC. It was found that DAS and DAC have different influence on the properties of biopolymeric scaffolds. Materials cross-linked with DAS were characterized by higher swelling ability (~4000% for DAS cross-linked materials; ~2500% for DAC cross-linked materials), they had lower density (Coll/CTS/30SF scaffold cross-linked with DAS: 21.8 ± 2.4 g/cm3; cross-linked with DAC: 14.6 ± 0.7 g/cm3) and lower mechanical properties (maximum deformation for DAC cross-linked scaffolds was about 69%; for DAS cross-linked scaffolds it was in the range of 12.67 ± 1.51% and 19.83 ± 1.30%) in comparison to materials cross-linked with DAC. Additionally, scaffolds cross-linked with DAS exhibited higher biocompatibility than those cross-linked with DAC. However, the obtained results showed that both types of scaffolds can provide the support required in regenerative medicine and tissue engineering. The scaffolds presented in the present work can be potentially used in bone tissue engineering to facilitate healing of small bone defects.

scholarly journals Functional silk fibroin hydrogels: preparation, properties and applications

2021 ◽  
Author(s):  
Haiyan Zheng ◽  
Baoqi Zuo
Keyword(s):  
Silk Fibroin ◽  
Silk Protein ◽  
Current Status ◽  
Protein Hydrogels

This article reviews the current status of the preparation, properties and application of functional silk protein hydrogels.

scholarly journals Investigation of the biological activity, mechanical properties and wound healing application of a novel scaffold based on lignin–agarose hydrogel and silk fibroin embedded zinc chromite nanoparticles

RSC Advances ◽  
2021 ◽  
Vol 11 (29) ◽  
pp. 17914-17923
Author(s):  
Reza Eivazzadeh-Keihan ◽  
Hooman Aghamirza Moghim Aliabadi ◽  
Fateme Radinekiyan ◽  
Mohammad Sobhani ◽  
Farzane khalili ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Wound Healing ◽  
Biological Activity ◽  
Silk Fibroin ◽  
Agarose Hydrogel ◽  
Novel Scaffold ◽  
Fibroin Solution ◽  
Zinc Chromite

Given the important aspects of wound healing approaches, in this work, an innovative biocompatible nanobiocomposite scaffold was designed and prepared based on cross-linked lignin–agarose hydrogel, extracted silk fibroin solution, and zinc chromite (ZnCr2O4) nanoparticles.

scholarly journals Cribellate thread production as model for spider’s spinneret kinematics

2021 ◽  
Author(s):  
Margret Weissbach ◽  
Marius Neugebauer ◽  
Anna-Christin Joel
Keyword(s):  
Molecular Structure ◽  
Mechanical Properties ◽  
Fibre Type ◽  
Material Science ◽  
Spider Silk ◽  
Functional Unit ◽  
Material Strength ◽  
Spinning Process ◽  
Fibre Spinning ◽  
House Spider

AbstractSpider silk attracts researchers from the most diverse fields, such as material science or medicine. However, still little is known about silk aside from its molecular structure and material strength. Spiders produce many different silks and even join several silk types to one functional unit. In cribellate spiders, a complex multi-fibre system with up to six different silks affects the adherence to the prey. The assembly of these cribellate capture threads influences the mechanical properties as each fibre type absorbs forces specifically. For the interplay of fibres, spinnerets have to move spatially and come into contact with each other at specific points in time. However, spinneret kinematics are not well described though highly sophisticated movements are performed which are in no way inferior to the movements of other flexible appendages. We describe here the kinematics for the spinnerets involved in the cribellate spinning process of the grey house spider, Badumna longinqua, as an example of spinneret kinematics in general. With this information, we set a basis for understanding spinneret kinematics in other spinning processes of spiders and additionally provide inspiration for biomimetic multiple fibre spinning.

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