Surface Modification for Protein Resistance Using a Biomimetic Approach

2003 ◽  
Vol 774 ◽  
Author(s):  
Jeffrey L. Dalsin ◽  
Phillip B. Messersmith
Keyword(s):  
High Concentration ◽  
Protein Resistance ◽  
Mussel Adhesive Proteins ◽  
Gold Substrates ◽  
Marine Mussels ◽  
Protein Adhesion ◽  
Biomimetic Approach ◽  
Mussel Adhesive ◽  
Poly Ethylene ◽  
Adhesive Proteins

AbstractIn recent years the immobilization of poly(ethylene glycol) (PEG) on surfaces has proved to be one of the most attractive methods to prevent biological fouling of surfaces. We have developed a paradoxical biomimetic PEGylation strategy that exploits the adhesive characteristics of proteins secreted by marine mussels—one of nature's most notorious foulers. Linear PEGs were coupled to peptides containing 3,4-dihydroxyphenylalanine (DOPA), an unusual amino acid which is found in high concentration in these so-called mussel adhesive proteins. Using surface plasmon resonance, we have demonstrated enhanced resistance to protein adhesion on gold substrates modified with the DOPA-containing PEGs.

A Biomimetic Approach to Enhancing Interfacial Interactions: Polydopamine-Coated Silica as Reinforcement for Epoxy Resin

2014 ◽  
Vol 1015 ◽  
pp. 721-724 ◽  
Author(s):  
Jian Li ◽  
Xue Mei Wen ◽  
Wei Zhang ◽  
Yu Ping Chen ◽  
Ying Xiao ◽  
...  
Keyword(s):  
Epoxy Resin ◽  
Stress Transfer ◽  
Interfacial Stress ◽  
Interfacial Interactions ◽  
Mussel Adhesive Proteins ◽  
Inorganic Composites ◽  
Biomimetic Approach ◽  
Biomimetic Method ◽  
Mussel Adhesive ◽  
Adhesive Proteins

A facile biomimetic method was developed to enhance the interfacial interaction in polymer-inorganic composites. By mimicking mussel adhesive proteins, a monolayer of polydopamine (PD) was constructed on surface of silica particles through a controllable coating pathway. The modified silica (PD-silica) was incorporated into an epoxy resin. It is found that the strong interfacial interactions brought by the polydopamine benefits the effective interfacial stress transfer, leading to greatly improved flexural properties of epoxy based composites.

scholarly journals Engineering of Biofilms with a Glycosylation Circuit for Biomaterial Applications

2021 ◽  
Author(s):  
Ebru Sahin Kehribar ◽  
Musa E İsilak ◽  
Eray U. Bozkurt ◽  
Jozef Adamcik ◽  
Raffaele Mezzenga ◽  
...  
Keyword(s):  
Spider Silk ◽  
Post Translational Modification ◽  
Adhesive Protein ◽  
Mussel Adhesive Proteins ◽  
Wide Range ◽  
Mussel Adhesive ◽  
Adhesive Proteins ◽  
Glycosylated Proteins

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....

Bioinspired Synthesis of Cross-Linking of Dopamine-Containing Block Copolymers to Form Thermosensitive Covalent Hydrogels

2012 ◽  
Vol 531-532 ◽  
pp. 238-241 ◽  
Author(s):  
Kui Huang ◽  
Jin San Chen ◽  
Yang Liu
Keyword(s):  
Sol Gel ◽  
Coupling Efficiency ◽  
Pluronic F127 ◽  
Cross Linking ◽  
Inversion Method ◽  
Sustained Drug Delivery ◽  
Vis Spectroscopy ◽  
Marine Mussels ◽  
Mussel Adhesive ◽  
Adhesive Proteins

Marine mussels secrete remarkable mussel adhesive proteins (MAPs) for adherence to the substrates upon which they reside. Inspired by the intermolecular cross-linking characteristics of MAPs, we report the synthesis of thermosensitive dopamine modified Pluronic copolymer (PluF127-Dopa) with high coupling efficiency. Under certain temperature and concentration, PluF127-Dopa copolymers in aqueous solution self-assemble into micelles and are able to rapidly form a more stable hydrogels upon addition of oxidizing reagents such as NaIO4, resulting from oxidative cross-linking of dopamine. UV-vis spectroscopy was utilized to identify the reaction intermediates. The sol-gel transition curves of cross-linked PluF127-Dopa hydrogels (CL-PluF127-Dopa) were determined by a vial inversion method. The critical gelation concentration of CL-PluF127-Dopa hydrogels was significantly lower than those for PluF127-Dopa and unmodified Pluronic F127. The apparent mechanical strength of CL-PluF127-Dopa hydrogels was dramatically enhanced compared to those unmodified Pluronic copolymer hydrogels, suitable for sustained drug delivery. These new biomimetic materials are expected to have potential uses in biomedical applications.

Complex coacervates based on recombinant mussel adhesive proteins: their characterization and applications

Soft Matter ◽  
2017 ◽  
Vol 13 (42) ◽  
pp. 7704-7716 ◽  
Author(s):  
Hyo Jeong Kim ◽  
Byeongseon Yang ◽  
Tae Yoon Park ◽  
Seonghye Lim ◽  
Hyung Joon Cha
Keyword(s):  
Practical Applications ◽  
Adhesive Protein ◽  
Underwater Adhesion ◽  
Significant Potential ◽  
Mussel Adhesive Proteins ◽  
Mussel Adhesive Protein ◽  
Mussel Adhesive ◽  
Adhesive Proteins

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

High Strength Underwater Bonding with Polymer Mimics of Mussel Adhesive Proteins

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

scholarly journals Expression of Functional Recombinant Mussel Adhesive Protein Mgfp-5 in Escherichia coli

2004 ◽  
Vol 70 (6) ◽  
pp. 3352-3359 ◽  
Author(s):  
Dong Soo Hwang ◽  
Hyo Jin Yoo ◽  
Jong Hyub Jun ◽  
Won Kyu Moon ◽  
Hyung Joon Cha
Keyword(s):  
Escherichia Coli ◽  
Adhesion Force ◽  
Soluble Form ◽  
Material Surface ◽  
Adhesive Properties ◽  
Affinity Ligand ◽  
Mussel Adhesive Proteins ◽  
Mussel Adhesive ◽  
Aqueous Conditions ◽  
Adhesive Proteins

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.

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