title: Cell adhesion biomaterial based on mussel adhesive protein fused with RGD peptide.
abstract: Previously, we designed and constructed a hybrid of the mussel adhesive protein (MAP) fp-151, which is a fusion protein with six type 1 (fp-1) decapeptide repeats at each type 5 (fp-5) terminus. Through various cell-adhesion analyses, we previously demonstrated that fp-151 has the potential to be used as a cell or tissue bioadhesive. In the present study, to improve the cell-adhesion properties of fp-151, we designed a new cell-adhesive protein, fp-151-RGD, which is a fusion with the GRGDSP residues, a RGD peptide sequence that has previously been identified at the cell-attachment site of fibronectin, at the C-terminus of fp-151. Although recombinant fp-151-RGD maintained the advantages associated with fp-151, such as a high production yield in Escherichia coli and simple purification, it showed superior spreading ability, which is important for cell proliferation under serum-free conditions, as well as better cell-adhesion ability compared with other commercially produced cell-adhesion materials such as poly-l-lysine (PLL) and the naturally extracted MAP mixture Cell-Tak. The excellent adhesion and spreading abilities of fp-151-RGD might be due to the fact that it utilizes three types of cell-binding mechanisms: DOPA adhesion of Cell-Tak, cationic binding force of PLL, and RGD sequence-mediated adhesion of fibronectin. Therefore, the new recombinant fp-151-RGD is suitable for use as a cell-adhesion material in cell culture or tissue engineering, and in any other area where efficient cell adhesion is required.
authors.affiliation: Department of Chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea.
authors.forename: Dong Soo
authors.initials: DS
authors.lastname: Hwang
authors.forename: Sung Bo
authors.initials: SB
authors.lastname: Sim
authors.forename: Hyung Joon
authors.initials: HJ
authors.lastname: Cha
mesh_terms: D000818:Animals; D016466:CHO Cells; D002448:Cell Adhesion / Q000502:physiology*; D049109:Cell Proliferation; D020099:Coated Materials, Biocompatible / Q000737:chemistry / Q000378:metabolism*; D006224:Cricetinae; D003412:Cricetulus; D004295:Dihydroxyphenylalanine / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D008422:Materials Testing; D018625:Microscopy, Atomic Force; D009842:Oligopeptides / Q000235:genetics / Q000378:metabolism*; D011506:Proteins / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013499:Surface Properties; D014443:Tyrosine / Q000378:metabolism
chemical_list: D020099:Coated Materials, Biocompatible; D009842:Oligopeptides; D011506:Proteins; D011993:Recombinant Fusion Proteins; C037403:adhesive protein, mussel; D014443:Tyrosine; D004295:Dihydroxyphenylalanine; C047981:arginyl-glycyl-aspartic acid