76 research outputs found

    Compartmental Modeling for the Neophyte: An Application of Berkeley Madonna

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    Compartmental modeling serves as a necessary framework in many fields, especially biomathematics and ecology. This article introduces readers to a user-friendly approach to constructing compartmental models and solving the resulting systems of differential equations to simulate real-world applications. The platform used is Berkeley Madonna, a software package that has an intuitive graphical interface which empowers users—even those with limited mathematical and programming backgrounds—to focus on modeling concepts rather than mathematical or programming intricacies. This makes Berkeley Madonna an ideal platform for students, educators, and researchers

    Fluorescence binding assay for a small peptide based on a GFP fusion protein

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    A fluorescence binding assay was developed for a small peptide based on a fusion protein between the peptide and the green fluorescent protein, GFP. The assay employs genetic engineering methods to prepare the analyte-label (peptide–GFP) conjugate as a fusion protein in order to produce a one-to-one, homogenous population of labeled-peptide. Specifically, a plasmid was constructed in which the C-terminus of a model octapeptide was fused to the N-terminus of GFP. Following expression of the octapeptide–GFP fusion protein in Escherichia coli, an immunoassay was developed based on sequential binding of the free octapeptide and labeled-octapeptide to an anti-octapeptide antibody immobilized on a solid surface. The naturally fluorescent protein acts as a label to provide sensitive detection for peptides. To our knowledge, this is the first time that GFP has been used as a quantitative label in a fusion protein to develop a quantitative assay for a peptide analyte

    A β‑Peptide Agonist of the GLP‑1 Receptor, a Class B GPCR

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    Previous work has shown that certain β(3)-peptides can effectively mimic the side chain display of an α-helix and inhibit interactions between proteins, both in vitro and in cultured cells. Here we describe a β(3)-peptide analog of GLP-1, CC-3(Act), that interacts with the GLP-1R extracellular domain (nGLP-1R) in vitro in a manner that competes with exendin-4 and induces GLP-1R-dependent cAMP signaling in cultured CHO-K1 cells expressing GLP-1R

    A β‑Peptide Agonist of the GLP‑1 Receptor, a Class B GPCR

    No full text
    Previous work has shown that certain β<sup>3</sup>-peptides can effectively mimic the side chain display of an α-helix and inhibit interactions between proteins, both <i>in vitro</i> and in cultured cells. Here we describe a β<sup>3</sup>-peptide analog of GLP-1, CC-3<sup>Act</sup>, that interacts with the GLP-1R extracellular domain (nGLP-1R) <i>in vitro</i> in a manner that competes with exendin-4 and induces GLP-1R-dependent cAMP signaling in cultured CHO-K1 cells expressing GLP-1R
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