Cation-induced shape programming and morphing in protein-based hydrogels

Khoury, Luai R.; Slawinski, Marina; Collison, Daniel R.; Popa, Ionel

doi:10.1126/sciadv.aba6112

Cited by 52 publications

(60 citation statements)

References 43 publications

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“…Of note, the C-like shape was particularly advantageous for pediatric patients, as it fits the growing airway by expanding [ 109 ]. The shape morphing capability of protein-based materials has also been observed with bovine serum albumin [ 110 , 111 ], calmodulin [ 112 ], and silk-elastin-like proteins [ 113 ], pointing to the development of 3D printing with shape-morphing protein-based materials.…”

Section: Methacryloyl-modificationmentioning

confidence: 99%

Photo-Crosslinked Silk Fibroin for 3D Printing

Sahoo

Cebe

et al. 2020

Polymers

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Silk fibroin in material formats provides robust mechanical properties, and thus is a promising protein for 3D printing inks for a range of applications, including tissue engineering, bioelectronics, and bio-optics. Among the various crosslinking mechanisms, photo-crosslinking is particularly useful for 3D printing with silk fibroin inks due to the rapid kinetics, tunable crosslinking dynamics, light-assisted shape control, and the option to use visible light as a biocompatible processing condition. Multiple photo-crosslinking approaches have been applied to native or chemically modified silk fibroin, including photo-oxidation and free radical methacrylate polymerization. The molecular characteristics of silk fibroin, i.e., conformational polymorphism, provide a unique method for crosslinking and microfabrication via light. The molecular design features of silk fibroin inks and the exploitation of photo-crosslinking mechanisms suggest the exciting potential for meeting many biomedical needs in the future.

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Section: Methacryloyl-modificationmentioning

confidence: 99%

Photo-Crosslinked Silk Fibroin for 3D Printing

Sahoo

Cebe

et al. 2020

Polymers

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Section: Protein Mechanics Has Made It Possible To Engineer Protein‐based Biomaterials To Mimic the Passive Elastic Properties Of Musclesmentioning

confidence: 99%

There Is Plenty of Room in The Folded Globular Proteins: Tandem Modular Elastomeric Proteins Offer New Opportunities in Engineering Protein‐Based Biomaterials

2021

Advanced NanoBiomed Research

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Shock absorber‐like elastomeric (SAE) proteins have become attractive building blocks to engineer protein hydrogels with tailored mechanical properties. These elastomeric proteins are tandem modular proteins consisting of individually folded globular domains and exhibit distinct mechanical properties. In response to stretching, folded globular domains can undergo force‐induced unfolding, leading to a significant change in protein stiffness and energy dissipation. These molecular behaviors of individual proteins can be harnessed and translated into macroscopic mechanical traits of protein hydrogels when such SAE proteins are used as building blocks to engineer protein hydrogels. These SAE proteins offer unique opportunities to rationally design protein‐based hydrogels by programming the mechanical properties of individual proteins at the molecular level, and thus help bridge the gap between biomechanics of macroscopic biomaterials and nanomechanics of single molecules.

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“…These changes can represent molecular mechanisms for adaptive behavior and signaling cascades. When binding to proteins, small ions such as divalent cations were shown to increase the mechanical stability of proteins [34,35]. For example, Ca 2+ release increases the overall stiffness of muscle titin [36] and the binding of Ca 2+ promotes domain refolding during bacterial adhesin [37].…”

Section: Architecture and Mechanisms Of Function Under Force For Protmentioning

confidence: 99%

Does protein unfolding play a functional role in vivo?

2020

Self Cite

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How mechanical unfolding of proteins has a functional role in vivo is still poorly understood. In this review, we distill the main biophysical characteristics of multidomain proteins functioning under force as binary molecular computational units and examine them as part of several biological processes. Understanding the relation between molecular unfolding of proteins under force and their overall macroscopic impact can provide insight into novel mechanical signaling pathways and gain‐of‐function mechanisms.

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Cation-induced shape programming and morphing in protein-based hydrogels

Cited by 52 publications

References 43 publications

Photo-Crosslinked Silk Fibroin for 3D Printing

Photo-Crosslinked Silk Fibroin for 3D Printing

There Is Plenty of Room in The Folded Globular Proteins: Tandem Modular Elastomeric Proteins Offer New Opportunities in Engineering Protein‐Based Biomaterials

Does protein unfolding play a functional role in vivo?

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