Expression of functional recombinant mussel adhesive protein Mgfp-5 in Escherichia coli.
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.
Hwang
Dong Soo
DS
Department of Chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea.
Yoo
Hyo Jin
HJ
Jun
Jong Hyub
JH
Moon
Won Kyu
WK
Cha
Hyung Joon
HJ
D000269:Adhesives; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D049872:Bivalvia / Q000378:metabolism*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D008422:Materials Testing; D018625:Microscopy, Atomic Force; D008969:Molecular Sequence Data; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016415:Sequence Alignment; D000267:Tissue Adhesions
D000269:Adhesives; D011506:Proteins; D011994:Recombinant Proteins; C037403:adhesive protein, mussel