Behavior of silk protein at the air–water interface

Yang, Yuhong; Dicko, Cedric; Bain, Colin D.; Gong, Zuguang; Jacobs, Robert M.; Shao, Zhengzhong; Terry, Ann E.; Vollrath, Fritz

doi:10.1039/c2sm26054a

Cited by 39 publications

(71 citation statements)

References 55 publications

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“…With the advent of single molecule manipulation techniques it is now possible to manipulate single proteins and study their 30 mechanical properties. The techniques include AFM, optical tweezers, magnetic tweezers and the biomembrane force probes 17,39 .…”

Section: Single Molecule Force Spectroscopy To Study Proteinsmentioning

confidence: 99%

“…The gradient of F U versus the natural logarithm of the pulling speed, gives a measure of the mechanical sensitivity of the protein to the speed at which 30 it is unfolded by force. Mechanically strong proteins such as rubredoxin (Fe-pfRD) exhibit a steep gradient, while mechanically weak proteins such as calmodulin (Cam DomC) exhibit a shallow gradient.…”

Section: Survey Of Single Molecule Protein Unfolding Datamentioning

confidence: 99%

“…In characterising the mechanical stability of a protein, it is common practice to perform single molecule force spectroscopy experiments at several different pulling speeds 65 . Generally, a dataset containing a large number of unfolding forces of a given 30 protein at a single pulling speed is plotted in the form of a histogram, and the median unfolding force value, and a measure of the spread of the data, are obtained ( Figures 5 A and B). This is repeated over several different pulling speeds, enabling the dependence of the force on the pulling speed to be plotted ( Figure 35 5 C).…”

Section: Single Molecule Force Spectroscopy To Study Proteinsmentioning

confidence: 99%

“…To exploit 25 proteins for the design of artificial, novel materials or to utilise them in nanomechanical systems as springs, switches or sensors 23 , it will be necessary to have a tool-box of proteins available with known or predictable mechanical properties. Although the number of experimentally studied proteins is ever 30 increasing, it is still very limited. Uncovering some of the design principles that underlie protein stability and flexibility is an important step towards achieving that goal.…”

Section: Introductionmentioning

confidence: 99%

“…These important processes range from the translocation of proteins/DNA across membranes 5,6 , the degradation of proteins by molecular 30 chaperone proteins 7 , the mechanical resilience of proteins within a molecular scaffold [8][9][10][11] and the conversion of mechanical signals into electrochemical signals 12, 13 ( Figure 1). In isolation or as a component of larger complexes, proteins perform their function through structural changes, modifying their intra-and 35 intermolecular interactions.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Towards design principles for determining the mechanical stability of proteins

Hoffmann

Tych

Hughes

et al. 2013

Phys. Chem. Chem. Phys.

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The successful integration of proteins into bionanomaterials with specific and desired function requires an accurate understanding of their material properties. Two such important properties are their mechanical stability and malleability. While single molecule manipulation techniques 15 now routinely provide access to these, there is a need to move towards predictive tools that can rationally identify proteins with desired material properties. We provide a comprehensive review of the available experimental data on the single molecule characterisation of proteins using the 20 atomic force microscope. We uncover a number of empirical relationships between the measured mechanical stability of a protein and its malleability which provide a set of simple tools which might be employed to estimate properties of previously uncharacterised proteins. 25

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Section: Single Molecule Force Spectroscopy To Study Proteinsmentioning

confidence: 99%

Section: Survey Of Single Molecule Protein Unfolding Datamentioning

confidence: 99%

Section: Single Molecule Force Spectroscopy To Study Proteinsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Towards design principles for determining the mechanical stability of proteins

Hoffmann

Tych

Hughes

et al. 2013

Phys. Chem. Chem. Phys.

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Recombinant Spider Silk Forms Tough and Elastic Nanomembranes that are Protein‐Permeable and Support Cell Attachment and Growth

Gustafsson

Tasiopoulos

Jansson

et al. 2020

Adv Funct Materials

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Biologically compatible membranes are of high interest for several biological and medical applications. Tissue engineering, for example, would greatly benefit from ultrathin, yet easy‐to‐handle, biodegradable membranes that are permeable to proteins and support cell growth. In this work, nanomembranes are formed by self‐assembly of a recombinant spider silk protein into a nanofibrillar network at the interface of a standing aqueous solution. The membranes are cm‐sized, free‐standing, bioactive and as thin as 250 nm. Despite their nanoscale thickness, the membranes feature an ultimate engineering strain of over 220% and a toughness of 5.2 MPa. Moreover, they are permeable to human blood plasma proteins and promote cell adherence and proliferation. Human keratinocytes seeded on either side of the membrane form a confluent monolayer within three days. The significance of these results lays in the unique combination of nanoscale thickness, elasticity, toughness, biodegradability, protein permeability and support for cell growth, as this may enable new applications in tissue engineering including bi‐layered in vitro tissue models and support for clinical transplantation of coherent cell layers.

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An Interfacial‐Assembled Self‐Supporting Nanofilm Induced by Strong Intermolecular Interaction between Silk Fibroin and Lysozyme

Miao,

Wang,

Liu

et al. 2024

Adv Funct Materials

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Organic ultrathin nanofilms are increasingly favored in a wide range of applications, including flexible photonics and electronics, smart skin devices, sensing, and bioinspired designs, due to their high flexibility, chemical activity, and stimuli‐responsiveness. To create large‐area, robust, and freestanding nanofilms efficiently, a protein interfacial cooperative assembly technique that utilizes silk fibroin and lysozyme as building blocks is developed. The strong intermolecular interaction between these two proteins, coupled with the abundant intra‐ and intermolecular β‐sheets, confers remarkable mechanical robustness to the nanofilms with thicknesses as low as 50 nm. Consequently, these nanofilms exhibit the unique ability to stand freely in the air and can be conformally transferred to substrates of different types and topographies, forming stable, and versatile nanocoatings. The advantageous attributes of their ultrathinness, large‐scale homogeneity, robustness, and rapid and tunable responsiveness facilitate the construction of ultrasensitive photonic architectures and organic–inorganic hybrid multilayers with outstanding optical and mechanical properties. It is envisioned that these all‐protein‐based robust nanofilms with unique nanoscale effects can be easily integrated into various advanced technological platforms to enable adaptive, multifunctional, and intelligent systems with exceptional mechanical strength.

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Behavior of silk protein at the air–water interface

Cited by 39 publications

References 55 publications

Towards design principles for determining the mechanical stability of proteins

Towards design principles for determining the mechanical stability of proteins

Recombinant Spider Silk Forms Tough and Elastic Nanomembranes that are Protein‐Permeable and Support Cell Attachment and Growth

An Interfacial‐Assembled Self‐Supporting Nanofilm Induced by Strong Intermolecular Interaction between Silk Fibroin and Lysozyme

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