muramidase and 16-mercaptohexadecanoic-acid

Diabetes arises from secretory defects in vascularized micro-organs known as the islets of Langerhans. Recent studies indicated that furthering our understanding of the paracrine effect of somatostatin on glucose-induced insulin secretion could represent a novel therapeutic avenue for diabetes. While many research groups are interested in insulin and glucagon secretion, few are particularly focused on studying the paracrine interaction in islets' cells, and none on monitoring a secretory fingerprint that contemplates more than two hormones. Surface plasmon resonance imaging can achieve high-throughput and multiplexed biomolecule quantification, making it an ideal candidate for detection of multiple islet's secretion products if arrays of hormones can be properly implemented on the sensing surface. In this study, we introduced a multiplex surface plasmon resonance imaging-based biosensor for simultaneous quantification of insulin, glucagon, and somatostatin. Performing this multiplex biosensing of hormones was mainly the result of the design of an antifouling sensing surface comprised by a mixed self-assembly monolayer of CH

Topics: Animals; Antibodies; Biofouling; Biosensing Techniques; Cattle; Glucagon; Humans; Immunoassay; Insulin; Limit of Detection; Muramidase; Palmitic Acids; Polyethylene Glycols; Serum Albumin, Bovine; Somatostatin; Surface Plasmon Resonance

Dip-pen nanolithography was used to construct arrays of proteins with 100- to 350-nanometer features. These nanoarrays exhibit almost no detectable nonspecific binding of proteins to their passivated portions even in complex mixtures of proteins, and therefore provide the opportunity to study a variety of surface-mediated biological recognition processes. For example, reactions involving the protein features and antigens in complex solutions can be screened easily by atomic force microscopy. As further proof-of-concept, these arrays were used to study cellular adhesion at the submicrometer scale.

Topics: 3T3 Cells; Adsorption; Animals; Cell Adhesion; Fibronectins; Focal Adhesions; Immunoglobulin G; Mice; Microscopy, Atomic Force; Miniaturization; Muramidase; Nanotechnology; Palmitic Acids; Protein Binding; Proteins; Receptor Aggregation; Recombinant Proteins