Exploring the Mesoscopic Morphology in Mussel Adhesive Proteins by Soft X-ray Spectromicroscopy

2021 ◽  
Author(s):  
Yuji Higaki ◽  
Kazutaka Kamitani ◽  
Takuji Ohigashi ◽  
Teruaki Hayakawa ◽  
Atsushi Takahara
2021 ◽  
Author(s):  
Ebru Sahin Kehribar ◽  
Musa E İsilak ◽  
Eray U. Bozkurt ◽  
Jozef Adamcik ◽  
Raffaele Mezzenga ◽  
...  

Glycosylation is a crucial post-translational modification for a wide range of functionalities. Adhesive protein-based biomaterials in nature rely on heavily glycosylated proteins such as spider silk and mussel adhesive proteins....


Soft Matter ◽  
2017 ◽  
Vol 13 (42) ◽  
pp. 7704-7716 ◽  
Author(s):  
Hyo Jeong Kim ◽  
Byeongseon Yang ◽  
Tae Yoon Park ◽  
Seonghye Lim ◽  
Hyung Joon Cha

Recombinant mussel adhesive protein-based complex coacervates are an effective underwater adhesive and have significant potential in practical applications that require underwater adhesion.


2017 ◽  
Vol 9 (8) ◽  
pp. 7866-7872 ◽  
Author(s):  
Michael A. North ◽  
Chelsey A. Del Grosso ◽  
Jonathan J. Wilker

2004 ◽  
Vol 70 (6) ◽  
pp. 3352-3359 ◽  
Author(s):  
Dong Soo Hwang ◽  
Hyo Jin Yoo ◽  
Jong Hyub Jun ◽  
Won Kyu Moon ◽  
Hyung Joon Cha

ABSTRACT Mussel adhesive proteins have been suggested as a basis for environmentally friendly adhesives for use in aqueous conditions and in medicine. However, attempts to produce functional and economical recombinant mussel adhesive proteins (mainly foot protein type 1) in several systems have failed. Here, the cDNA coding for Mytilus galloprovincialis foot protein type 5 (Mgfp-5) was isolated for the first time. Using this cDNA, we produced a recombinant Mgfp-5 fused with a hexahistidine affinity ligand, which was expressed in a soluble form in Escherichia coli and was highly purified using affinity chromatography. The adhesive properties of purified recombinant Mgfp-5 were compared with the commercial extracted mussel adhesive Cell-Tak by investigating adhesion force using atomic force microscopy, material surface coating, and quartz crystal microbalance. Even though further macroscale assays are needed, these microscale assays showed that recombinant Mgfp-5 has significant adhesive ability and may be useful as a bioadhesive in medical or underwater environments.


2020 ◽  
Vol 164 ◽  
pp. 108351 ◽  
Author(s):  
Jie Cheng ◽  
Sulin Chen ◽  
Fan Zhang ◽  
Bin Shen ◽  
Xinchun Lu ◽  
...  

2020 ◽  
Vol 11 (1) ◽  
pp. 19 ◽  
Author(s):  
Simona Zuppolini ◽  
Iriczalli Cruz-Maya ◽  
Vincenzo Guarino ◽  
Anna Borriello

In recent years, mussel adhesive proteins have attracted much attention because they can form strong adhesive interface interactions with various substrates in a wet environment. Inspired by their catechol- and amine-based molecular structure, polydopamine (PDA), a dopamine derived synthetic eumelanin polymer, was recognized as a suitable bio-interface coating. PDA was successfully used to improve adhesion due to the availability of copious functional groups for covalently immobilizing biomolecules and anchoring reactive species and ions. Recently, it has been demonstrated that PDA and its derivatives can be successfully used for the surface modification of implants interfaces to modulate in vitro cellular responses in order to enhance the in vivo functionality of biomedical implants (i.e., prosthesis). Herein, we propose the development of multifunctional scaffolds based on polyε–caprolactone (PCL) electrospun fibers coated with PDA via electro fluid dynamic methods, by optimizing polymerization/oxidation reactions capable of driving PDA self–assembly, and, ultimately, investigating the effects on cell response. Morphological analyses have confirmed the possibility to obtain different surface topographies as a function of the coating process while in vitro studies proved the ability of PDA coating to interact with cells no compromising in vitro viability. In perspective, in vitro conductive properties of fibers will be further investigated in order to validate their promising use as bioconductive interfaces for tissue engineering applications.


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