Self-assembled adhesive biomaterials formed by a genetically designed fusion protein

2018 ◽  
Vol 54 (89) ◽  
pp. 12642-12645 ◽  
Author(s):  
Pulakesh Aich ◽  
Jaeyeon An ◽  
Byeongseon Yang ◽  
Young Ho Ko ◽  
Junghyun Kim ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Adhesion Property ◽  
Underwater Adhesion ◽  
Genetic Fusion ◽  
Self Assembled ◽  
Mussel Foot Protein

A spider with mussel: a supramolecular fiber formed by a spider dragline protein was tuned to have underwater adhesion property by genetic fusion of a mussel foot protein.

Cell-Permeable, MMP-2 Activatable, Nickel Ferrite and His-Tagged Fusion Protein Self-Assembled Fluorescent Nanoprobe for Tumor Magnetic-Targeting and Imaging

2017 ◽  
Vol 9 (45) ◽  
pp. 39209-39222 ◽  
Author(s):  
Lu Sun ◽  
Shuping Xie ◽  
Jing Qi ◽  
Ergang Liu ◽  
Di Liu ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Nickel Ferrite ◽  
Magnetic Targeting ◽  
Fluorescent Nanoprobe ◽  
Self Assembled

A Biosynthetic Hybrid Spidroin-Amyloid-Mussel Foot Protein for Underwater Adhesion on Diverse Surfaces

2021 ◽  
Author(s):  
Eugene Kim ◽  
Juya Jeon ◽  
Yaguang Zhu ◽  
Ethan D. Hoppe ◽  
Young-Shin Jun ◽  
...  
Keyword(s):  
Underwater Adhesion ◽  
Mussel Foot Protein

Development of a Multifunctional Nanobiointerface Based on Self-Assembled Fusion-Protein rSbpA/ZZ for Blood Cell Enrichment and Phenotyping

2017 ◽  
Vol 9 (39) ◽  
pp. 34423-34434 ◽  
Author(s):  
Mario Rothbauer ◽  
Martin Frauenlob ◽  
Karoline Gutkas ◽  
Michael B. Fischer ◽  
Eva-Kathrin Sinner ◽  
...  
Keyword(s):  
Blood Cell ◽  
Fusion Protein ◽  
Cell Enrichment ◽  
Self Assembled

scholarly journals Multimodal underwater adhesion using self-assembled Dopa-bearing ABA triblock copolymer networks

2018 ◽  
Vol 6 (4) ◽  
pp. 545-549 ◽  
Author(s):  
Xiaomin Tang ◽  
Christopher J. Bettinger
Keyword(s):  
Energy Dissipation ◽  
Triblock Copolymer ◽  
Interfacial Bonding ◽  
Underwater Adhesion ◽  
Aba Triblock Copolymer ◽  
Self Assembled

Self-assembled mechanically robust Dopa-bearing triblock copolymer networks improve underwater adhesion through both energy dissipation and interfacial bonding.

scholarly journals Simple peptide coacervates adapted for rapid pressure-sensitive wet adhesion

Soft Matter ◽  
2017 ◽  
Vol 13 (48) ◽  
pp. 9122-9131 ◽  
Author(s):  
Ilia Kaminker ◽  
Wei Wei ◽  
Alex M. Schrader ◽  
Yeshayahu Talmon ◽  
Megan T. Valentine ◽  
...  
Keyword(s):  
Thin Films ◽  
Single Component ◽  
Wet Adhesion ◽  
Underwater Adhesion ◽  
Pressure Sensitive ◽  
Mussel Foot Protein ◽  
Rapid Pressure

Single-component peptide coacervates mimicking mussel foot protein-3S were adapted for rapid pressure-sensitive wet adhesion. The coacervate upon compression exhibited orders of magnitude higher underwater adhesion at 2 N m−1 than thin films of the most adhesive mussel-foot-derived peptides reported to date.

scholarly journals Self-Assembled Amyloid-Like Oligomeric-Cohesin Scaffoldin for Augmented Protein Display on the Saccharomyces cerevisiae Cell Surface

2012 ◽  
Vol 78 (9) ◽  
pp. 3249-3255 ◽  
Author(s):  
Zhenlin Han ◽  
Bei Zhang ◽  
Yi E. Wang ◽  
Yi Y. Zuo ◽  
Wei Wen Su
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Surface ◽  
Fusion Protein ◽  
Fold Increase ◽  
Scaffolding Protein ◽  
Yeast Display ◽  
Protein Scaffold ◽  
Content Type ◽  
Self Assembled ◽  
Novel Protein

ABSTRACTIn this study, a molecular self-assembly strategy to develop a novel protein scaffold for amplifying the extent and variety of proteins displayed on the surface ofSaccharomyces cerevisiaeis presented. The cellulosomal scaffolding protein cohesin and its upstream hydrophilic domain (HD) were genetically fused with the yeast Ure2p N-terminal fibrillogenic domain consisting of residues 1 to 80 (Ure2p1-80). The resulting Ure2p1-80-HD-cohesin fusion protein was successfully expressed inEscherichia colito produce self-assembled supramolecular nanofibrils that serve as a novel protein scaffold displaying multiple copies of functional cohesin domains. The amyloid-like property of the nanofibrils was confirmed via thioflavin T staining and atomic force microscopy. These cohesin nanofibrils attached themselves, via a green fluorescent protein (GFP)-dockerin fusion protein, to the cell surface ofS. cerevisiaeengineered to display a GFP-nanobody. The excess cohesin units on the nanofibrils provide ample sites for binding to dockerin fusion proteins, as exemplified using an mCherry-dockerin fusion protein as well as theClostridium cellulolyticumCelA endoglucanase. More than a 24-fold increase in mCherry fluorescence and an 8-fold increase in CelA activity were noted when the cohesin nanofibril scaffold-mediated yeast display was used, compared to using yeast display with GFP-cohesin that contains only a single copy of cohesin. Self-assembled supramolecular cohesin nanofibrils created by fusion with the yeast Ure2p fibrillogenic domain provide a versatile protein scaffold that expands the utility of yeast cell surface display.

scholarly journals Pseudo-Zwitterions Self-Assembled from Polycation and Anion-Clusters Showing Exceptional Water-Cleanable Anti-Crude Oil Adhesion Property

iScience ◽  
2021 ◽  
pp. 102964
Author(s):  
Yuzhang Zhu ◽  
Hongzhen Lin ◽  
Wangxi Fang ◽  
Aqiang Wang ◽  
Jichao Sun ◽  
...  
Keyword(s):  
Crude Oil ◽  
Adhesion Property ◽  
Anion Clusters ◽  
Self Assembled

scholarly journals Tropoelastin-Inspired, Non-Ionic, Self-Coacervating Polyesters as Strong Underwater Adhesives

2019 ◽  
Author(s):  
Amal Narayanan ◽  
Joshua Menefee ◽  
Qianhui Liu ◽  
Ali Dhinojwala ◽  
Abraham Joy
Keyword(s):  
Functional Groups ◽  
Tissue Adhesives ◽  
Underwater Adhesion ◽  
Wide Range ◽  
External Conditions ◽  
The One ◽  
Mussel Foot Protein ◽  
Potential Use ◽  
Enhanced Stability ◽  
Modular Nature

Inspired from the one-component self-coacervation of tropoelastin and mussel foot protein-3s, we created the first non-ionic, single component coacervates that can coacervate in a all ranges of pH (acidic to basic) and wide range of ionic strengths with degradability, rapid curing and strong underwater adhesion. In contrast to the complex coacervates, these ‘charge-free’ coacervates are potential candidates as tissue adhesives and sealants, adhesives for sensor attachment to wet skin, and as sprayable adhesives. Their potential use in the clinic arises from their enhanced stability to changes in external conditions, cytocompatibility, biodegradability and modular nature in incorporating various functional groups and crosslinkers.

scholarly journals Tropoelastin-Inspired, Non-Ionic, Self-Coacervating Polyesters as Strong Underwater Adhesives

2019 ◽  
Author(s):  
Amal Narayanan ◽  
Joshua Menefee ◽  
Qianhui Liu ◽  
Ali Dhinojwala ◽  
Abraham Joy
Keyword(s):  
Functional Groups ◽  
Tissue Adhesives ◽  
Underwater Adhesion ◽  
Wide Range ◽  
External Conditions ◽  
The One ◽  
Mussel Foot Protein ◽  
Potential Use ◽  
Enhanced Stability ◽  
Modular Nature

Inspired from the one-component self-coacervation of tropoelastin and mussel foot protein-3s, we created the first non-ionic, single component coacervates that can coacervate in a all ranges of pH (acidic to basic) and wide range of ionic strengths with degradability, rapid curing and strong underwater adhesion. In contrast to the complex coacervates, these ‘charge-free’ coacervates are potential candidates as tissue adhesives and sealants, adhesives for sensor attachment to wet skin, and as sprayable adhesives. Their potential use in the clinic arises from their enhanced stability to changes in external conditions, cytocompatibility, biodegradability and modular nature in incorporating various functional groups and crosslinkers.

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