Multifunctional polyampholyte hydrogels with fouling resistance and protein conjugation capacity.

Materials that are resistant to nonspecific protein adsorption are critical in the biomedical community. Specifically, nonfouling implantable biomaterials are necessary to reduce the undesirable, but natural foreign body response. The focus of this investigation is to demonstrate that polyampholyte hydrogels prepared with equimolar quantities of positively charged [2-(acryloyloxy)ethyl] trimethylammonium chloride (TMA) and negatively charged 2-carboxyethyl acrylate (CAA) monomers are a viable solution to this problem.

Mineralization induction effects of osteopontin, bone sialoprotein, and dentin phosphoprotein on a biomimetic collagen substrate.

Native bone tissue is composed of a matrix of collagen, noncollagenous proteins, and calcium phosphate minerals, which are primarily hydroxyapatite. The SIBLING (small integrin-binding ligand, N-linked glycoprotein) family of proteins is the primary noncollagenous protein group found in mineralized tissues. In this work, the mineralization induction capabilities of three of the SIBLING members, bone sialoprotein (BSP), osteopontin (OPN), and the calcium-binding subdomain of dentin sialophosphoprotein, dentin phosphoprotein (DPP), are directly compared on a biomimetic collagen substrate.

Tailoring the protein adsorption properties of whispering gallery mode optical biosensors.

Label-free biosensor technologies have the potential to revolutionize environmental monitoring, medical diagnostics, and food safety evaluation processes due to their unique combinations of high-sensitivity signal transducers and high-specificity recognition elements. This enables their ability to perform real-time detection of deleterious compounds at extremely low concentrations. However, to further improve the biosensors' performance in complex environments, such as wastewater, blood, and urine, it is necessary to minimize nonspecific binding, which in turn will increase their specificity, and decrease the rate of false positives.

Adhesion of MC3T3-E1 cells bound to dentin phosphoprotein specifically bound to collagen type I.

Dentin sialophosphoprotein (DSPP) is a member of the SIBLING (small integrin binding N-linked glycoprotein) family of proteins commonly found in mineralized tissues. Dentin phosphoprotein (DPP) is a naturally occurring subdomain of DSPP that contains the cell binding RGD sequence. Previously, the orientation and conformation of other SIBLING family members specifically bound to collagen I have been investigated with respect to their cell adhesion properties.