Recombinant mussel adhesive protein as a gene delivery material

Hwang, Dong Soo; Kim, Kyoung Ro; Lim, Seonghye; Choi, Yanghee; Joon, Hyung

doi:10.1002/bit.22086

Cited by 12 publications

(12 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The PCR product was digested with NcoI and XhoI, and the digested DNA fragment was ligated into a pET22b(+) vector (Novagen, Darmstadt, Germany) predigested with NcoI and XhoI to make the recombinant plasmid pET‐MAP. The gene encoding the B and C domains of protein A was amplified by PCR from the genomic DNA of Staphylococcus aureus ATCC 6538 46. The forward primer (F2: 5'‐GCG C CA TAT G GA TAA CAA ATT CAA CAA AGA ACA AC‐ 3 ') was designed to contain an NdeI restriction‐enzyme site and the backward primer (B2: 5'‐GCG C CC ATG G TT TTG GTG CTT GAG CAT CGT TTA GC‐ 3 ') was designed to contain an NcoI restriction‐enzyme site.…”

Section: Methodsmentioning

confidence: 99%

A Mussel Adhesive Protein Fused with the BC Domain of Protein A is a Functional Linker Material that Efficiently Immobilizes Antibodies onto Diverse Surfaces

Kim

Choi

et al. 2011

Adv Funct Materials

Self Cite

View full text Add to dashboard Cite

The efficient immobilization of antibodies onto solid surfaces is vital for the sensitivity and specificity of various immunoassays and immunosensors. A novel linker protein, BC‐MAP, is designed and produced in Escherichia coli by genetically fusing mussel adhesive protein (MAP) with two domains (B and C) of protein A (antibody‐binding protein) for efficient antibody immobilization on diverse surfaces. Through direct surface‐coating analyses, it is found that BC‐MAP successfully coats diverse surfaces including glass, polymers, and metals, but the BC domain alone does not. Importantly, antibodies are efficiently immobilized on BC‐MAP‐coated surfaces, and the immobilized antibodies interact selectively with their corresponding antigen. Quartz‐crystal‐microbalance analyses show that BC‐MAP has excellent antibody‐binding ability compared to that of BC protein on gold surfaces. These results demonstrate that the MAP domain, with uniquely strong underwater adhesive properties, plays a role in the direct and efficient coating of BC‐MAP molecules onto diverse surfaces that lack additional surface treatment, and the BC domain of BC‐MAP contributes to the selective and oriented immobilization of antibodies on BC‐MAP‐coated surfaces. Thus, the BC‐MAP fusion protein could be a valuable novel linker material for the facile and efficient immobilization of antibodies onto diverse solid supports.

show abstract

Section: Methodsmentioning

confidence: 99%

A Mussel Adhesive Protein Fused with the BC Domain of Protein A is a Functional Linker Material that Efficiently Immobilizes Antibodies onto Diverse Surfaces

Kim

Choi

et al. 2011

Adv Funct Materials

Self Cite

View full text Add to dashboard Cite

show abstract

“…Surface engineering strategies have also been applied for the design of drug carrier to improve transfection efficiency and increase the bioactivity of their cargo . Recombinant MAP fp‐151‐based nucleic acid immobilization has been proposed for effective transfection via the electrostatic interaction between positively charged fp‐151 and negatively charged DNA . The mixture of fp‐151 and DNA achieved complete immobilization at a ratio of 4:1 (w/w) for fp‐151:DNA.…”

Section: Applications Of Recombinant Map‐based Surface Engineeringmentioning

confidence: 99%

Biomimetic Surface Engineering of Biomaterials by Using Recombinant Mussel Adhesive Proteins

Kim

Jeong

et al. 2018

Adv Materials Inter

Self Cite

View full text Add to dashboard Cite

Surface engineering is a key approach for tailoring new functionalities into biomaterials to achieve better clinical performance. The rise of genetic engineering and molecular biotechnology made it possible to design artificial sticky proteins derived from marine mussels that are capable of firmly anchoring on a variety of substrates with high binding strength, opening a new route for surface engineering of biomaterials. Coatings of recombinant mussel adhesive proteins (MAPs) have aroused great interest for the surface functionalization of biomaterials due to their simplicity, versatility, and high stability under physiological conditions, as well as their favorable interactions with cells. In addition, recombinant MAPs can be engineered to provide desired specific functionalities on target surfaces by genetic fusion with functional peptides and/or by the immobilization of biomolecules. This review provides an overview of recombinant MAPs‐based surface coatings, highlighting their mechanisms, characteristic surface properties, and diverse applications in providing bioengineered surfaces in the fields of biomedical and tissue engineering.

show abstract

“…These characteristics make the two hybrid proteins fp-151 and fp-151-RGD suitable for use as cell-adhesion material in cell culture or tissue engineering [97]. In a totally different context, fp-151 has been proposed as a potential gene delivery material in view of its similarity of amino acid composition to histone proteins, which are known as effective mediators of transfection [65]. The fusion protein displayed comparable transfection efficiency in human and mouse cells compared to the widely used transfection agent Lipofectamine (Invitrogen).…”

Section: Applicationsmentioning

confidence: 99%