Adding Functions to Biomaterial Surfaces through Protein Incorporation

Abstract

The concept of biomaterials has evolved from one of inert mechanical supports with a long-term, biologically inactive role in the body into complex matrices that exhibit selective cell binding, promote proliferation and matrix production, and may ultimately become replaced by newly generated tissues in vivo. Functionalization of material surfaces with biomolecules is critical to their ability to evade immunorecognition, interact productively with surrounding tissues and extracellular matrix, and avoid bacterial colonization. Antibody molecules and their derived fragments are commonly immobilized on materials to mediate coating with specific cell types in fields such as stent endothelialization and drug delivery. The incorporation of growth factors into biomaterials has found application in promoting and accelerating bone formation in osteogenerative and related applications. Peptides and extracellular matrix proteins can impart biomolecule- and cell-specificities to materials while antimicrobial peptides have found roles in preventing biofilm formation on devices and implants. In this progress report, we detail developments in the use of diverse proteins and peptides to modify the surfaces of hard biomaterials in vivo and in vitro. Chemical approaches to immobilizing active biomolecules are presented, as well as platform technologies for isolation or generation of natural or synthetic molecules suitable for biomaterial functionalization.

Differentiation of Bone Marrow Stem Cells into Schwann Cells for the Promotion of Neurite Outgrowth on Electrospun Fibers

“…26,39–41 The presence of proteins on their surface can also modulate the interactions between the fibers and the cells, thereby affecting the differentiation of stem cells. 42,43 …”

Orientation and characterization of immobilized antibodies for improved immunoassays (Review)

“…However, it is likely that smaller antibody fragments and aptamers may be favored over whole antibodies in the future as they can be prepared recombinantly and are easily modified genetically or chemically with the ability to maximize capture events due to increased packing and binding site density. 168 Additionally, camelid antibodies with one single domain for antigen binding (known as VHH) have attracted attention due to their high solubility and stability, and may provide an opportunity for incorporation into sensors. 8 Also, peptides and aptamers provide a highly customizable method for producing covalent attachment of antibodies, or fragments thereof, either by active targeting of the protein, or the substrate, or both.…”

Binding efficiency of recombinant collagen‐binding basic fibroblast growth factors (CBD‐bFGFs) and their promotion for NIH‐3T3 cell proliferation

“…Growth factors with affinity tags supplied by recombinant expression and ligase could promote incorporation between growth factors with biomaterials through affinity domains from antibodies, enzymes, and other bio‐macromolecules . The bioactivity of growth factors has been found effective with its dosage and the peak bioactivity is obtained at a certain dosage called maximal effective dose (MED).…”

“…[2,3] The method of adsorption/physisorption governed by hydrophobic, hydration and electrostatic force is greatly used for non-sitespecific approach of growth factors to materials. [4] On the other hand, attachment of growth factors to biomaterials (eg, polymers, metals, ceramics and composites) is enhanced by surface modification, [5][6][7] covalent bonding, [8][9][10][11] encapsulating, [12][13][14] and biomaterial-binding growth factors. [2,[15][16][17][18] Recently, a method to capture endogenous growth factors onto biomaterials by growth-factor-binding peptides was employed to overcome the supraphysiological doses for exogenous administration of growth factors.…”

“…Growth factors with affinity tags supplied by recombinant expression and ligase could promote incorporation between growth factors with biomaterials through affinity domains from antibodies, enzymes, and other bio-macromolecules. [4] The bioactivity of growth factors has been found effective with its dosage and the peak bioactivity is obtained at a certain dosage called maximal effective dose (MED). The dosage of growth factors is normally expressed by its concentration in the medium (eg, bFGF) when applied with soluble method (for instance, the dosage for medium of human skin fibroblasts is about 100 pM [20] ).…”