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      Next-generation protein-based materials capture and preserve projectiles from supersonic impacts

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          Abstract

          Extreme energy-dissipating materials are essential for a range of applications. The military and police force require ballistic armour to ensure the safety of their personnel, while the aerospace industry requires materials that enable the capture, preservation and study of hypervelocity projectiles. However, current industry standards display at least one inherent limitation, such as weight, breathability, stiffness, durability and failure to preserve captured projectiles. To resolve these limitations, we have turned to nature, using proteins that have evolved over millennia to enable effective energy dissipation. Specifically, a recombinant form of the mechanosensitive protein talin was incorporated into a monomeric unit and crosslinked, resulting in a talin shock-absorbing material (TSAM). When subjected to 1.5 km s −1 supersonic shots, TSAMs were shown to absorb the impact and capture and preserve the projectile.

          Abstract

          An engineered version of the mechanosensitive protein talin was used as a monomer in combination with a synthetic chemical crosslinker to form a hydrogel. This shock-absorbing material is shown to capture and preserve projectiles fired at 1.5 km s −1.

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          Most cited references34

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          The use and misuse of FTIR spectroscopy in the determination of protein structure.

          Fourier transform infrared (FTIR) spectroscopy is an established tool for the structural characterization of proteins. However, many potential pitfalls exist for the unwary investigator. In this review we critically assess the application of FTIR spectroscopy to the determination of protein structure by (1) outlining the principles underlying protein secondary structure determination by FTIR spectroscopy, (2) highlighting the situations in which FTIR spectroscopy should be considered the technique of choice, (3) discussing the manner in which experiments should be conducted to derive as much physiologically relevant information as possible, and (4) outlining current methods for the determination of secondary structure from infrared spectra of proteins.
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            The mechanical response of talin

            Talin, a force-bearing cytoplasmic adapter essential for integrin-mediated cell adhesion, links the actin cytoskeleton to integrin-based cell–extracellular matrix adhesions at the plasma membrane. Its C-terminal rod domain, which contains 13 helical bundles, plays important roles in mechanosensing during cell adhesion and spreading. However, how the structural stability and transition kinetics of the 13 helical bundles of talin are utilized in the diverse talin-dependent mechanosensing processes remains poorly understood. Here we report the force-dependent unfolding and refolding kinetics of all talin rod domains. Using experimentally determined kinetics parameters, we determined the dynamics of force fluctuation during stretching of talin under physiologically relevant pulling speeds and experimentally measured extension fluctuation trajectories. Our results reveal that force-dependent stochastic unfolding and refolding of talin rod domains make talin a very effective force buffer that sets a physiological force range of only a few pNs in the talin-mediated force transmission pathway.
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              Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation

              The force-dependent interaction between talin and vinculin plays a crucial role in the initiation and growth of focal adhesions. Here we use magnetic tweezers to characterise the mechano-sensitive compact N-terminal region of the talin rod, and show that the three helical bundles R1–R3 in this region unfold in three distinct steps consistent with the domains unfolding independently. Mechanical stretching of talin R1–R3 enhances its binding to vinculin and vinculin binding inhibits talin refolding after force is released. Mutations that stabilize R3 identify it as the initial mechano-sensing domain in talin, unfolding at ∼5 pN, suggesting that 5 pN is the force threshold for vinculin binding and adhesion progression.
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                Author and article information

                Contributors
                J.R.Hiscock@kent.ac.uk
                B.T.Goult@kent.ac.uk
                Journal
                Nat Nanotechnol
                Nat Nanotechnol
                Nature Nanotechnology
                Nature Publishing Group UK (London )
                1748-3387
                1748-3395
                3 July 2023
                3 July 2023
                2023
                : 18
                : 9
                : 1060-1066
                Affiliations
                [1 ]School of Biosciences, University of Kent, ( https://ror.org/00xkeyj56) Canterbury, UK
                [2 ]School of Chemistry and Forensic Science, University of Kent, ( https://ror.org/00xkeyj56) Canterbury, UK
                [3 ]Department of Physics, Chiba University, ( https://ror.org/01hjzeq58) Chiba, Japan
                [4 ]School of Physics and Astronomy, University of Kent, ( https://ror.org/00xkeyj56) Canterbury, UK
                [5 ]Present Address: Department of Chemistry, University of Southampton, ( https://ror.org/01ryk1543) Southampton, UK
                Author information
                http://orcid.org/0000-0001-9892-281X
                http://orcid.org/0000-0001-6162-8895
                http://orcid.org/0000-0001-6138-1028
                http://orcid.org/0000-0002-1406-8802
                http://orcid.org/0000-0002-3438-2807
                Article
                1431
                10.1038/s41565-023-01431-1
                10501900
                37400719
                d071c6a2-005d-4dfc-ac4b-5c79c2056cf1
                © The Author(s) 2023

                Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

                History
                : 1 December 2022
                : 19 May 2023
                Funding
                Funded by: FundRef https://doi.org/10.13039/501100000268, RCUK | Biotechnology and Biological Sciences Research Council (BBSRC);
                Award ID: BB/S007245/1
                Award Recipient :
                Funded by: FundRef https://doi.org/10.13039/501100000289, Cancer Research UK (CRUK);
                Award ID: DRCRPG-May21
                Award Recipient :
                Funded by: FundRef https://doi.org/10.13039/501100001316, University of Kent;
                Funded by: FundRef https://doi.org/10.13039/501100000271, RCUK | Science and Technology Facilities Council (STFC);
                Award ID: ST/S000348/1
                Award Recipient :
                Funded by: UKRI - MR/T020415/1
                Categories
                Article
                Custom metadata
                © Springer Nature Limited 2023

                Nanotechnology
                biomaterials,polymer chemistry
                Nanotechnology
                biomaterials, polymer chemistry

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