Development of a Porous Silicon Based Biosensor

1998 ◽  
Vol 536 ◽  
Author(s):  
Keiki-Pua S. Dancil ◽  
Douglas P. Greiner ◽  
Michael J. Sailor

AbstractIn this paper we demonstrate that porous silicon (PS) can be used as an immobilization matrix and a transducer for biosensor applications. Thin layers of PS were fabricated showing fine structure in their reflection spectra, characteristic of longitudinal optical cavity modes, or Fabry-Perot interference fringes. The PS surface was modified by covalently bonding streptavidin to a heterobifunctional linker immobilized to the surface using common silane chemistry. The mode spacing and wavelength in the interference spectrum was modified, by displacing buffer and introducing proteins into the PS layer. Protein-protein interactions between immobilized Streptavidin and biotinylated Protein A followed by Protein A and IgG were detected. The surface was regenerated during the course of the experiment showing reversibility of the sensor at the third layer.

1993 ◽  
Vol 298 ◽  
Author(s):  
Vincent V. Doan ◽  
C. L. Curtis ◽  
G. M. Credo ◽  
M. J. Sailor ◽  
R. M. Penner

AbstractUniform layers of porous silicon have been produced in a photoelectrochemical etch that show intensity enhancements of up to 100 fold, relative to samples etched in the dark. These films can also show fine structure in their photoluminescence (PL) spectra characteristic of longitudinal optical cavity modes. The highly luminescent, uniform porous layer is generated by illumination with blue or green light during the electrochemical etch of singlecrystal (B-doped) Si, and the enhancement is attributed to a localized photochemical etch process. The relevance of the increased PL intensity and interference-induced spectral changes to measurements of the intrinsic emission spectrum of porous Si are discussed.


2021 ◽  
Vol 12 (1) ◽  
pp. 420-430

Host microbial interactions had significant factors in maintains homeostasis and immune-related activity. One such interaction made by Lactobacillus sp. with Surface layer proteins (Slps) had been studied through a computational approach. Erb3 and αIIB-β3, which are epithelial surface layer receptors, are subjected to interact with the Slp homology model. Both cell surface receptors were subjected to interact through computational docking, followed by molecular dynamics simulations through the coarse-grain method to explore the conformational stability. Through the implementation of the molecular docking for the surface layer protein A, we have shown the surface layer protein A, protein-protein interactions are higher in cellular receptors with epidermal growth factor receptor at an -34.45 ΔG and -51.19 ΔG through molecular docking with Erb3 and αIIB-β3. This study shows the unique interaction of Slp with the epithelial surface receptors like Erb3 and αIIB-β3, which are multipurpose applications in microbial-based drug therapeutics.


1993 ◽  
Vol 140 (12) ◽  
pp. 3492-3494 ◽  
Author(s):  
Corrine L. Curtis ◽  
Vincent V. Doan ◽  
Grace M. Credo ◽  
Michael J. Sailor

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Jie Chen ◽  
Nan Liu ◽  
Yinpin Huang ◽  
Yuanxun Wang ◽  
Yuxing Sun ◽  
...  

AbstractMolecular glues are a class of small molecular drugs that mediate protein-protein interactions, that induce either the degradation or stabilization of target protein. A structurally diverse group of chemicals, including 17-β-estradiol (E2), anagrelide, nauclefine, and DNMDP, induces apoptosis by forming complexes with phosphodiesterase 3A (PDE3A) and Schlafen 12 protein (SLFN12). They do so by binding to the PDE3A enzymatic pocket that allows the compound-bound PDE3A to recruit and stabilize SLFN12, which in turn blocks protein translation, leading to apoptosis. In this work, we report the high-resolution cryo-electron microscopy structure of PDE3A-SLFN12 complexes isolated from cultured HeLa cells pre-treated with either anagrelide, or nauclefine, or DNMDP. The PDE3A-SLFN12 complexes exhibit a butterfly-like shape, forming a heterotetramer with these small molecules, which are packed in a shallow pocket in the catalytic domain of PDE3A. The resulting small molecule-modified interface binds to the short helix (E552-I558) of SLFN12 through hydrophobic interactions, thus “gluing” the two proteins together. Based on the complex structure, we designed and synthesized analogs of anagrelide, a known drug used for the treatment of thrombocytosis, to enhance their interactions with SLFN12, and achieved superior efficacy in inducing apoptosis in cultured cells as well as in tumor xenografts.


2019 ◽  
Vol 132 ◽  
pp. 143-161 ◽  
Author(s):  
Ie Mei Bhattacharyya ◽  
Shira Cohen ◽  
Awad Shalabny ◽  
Muhammad Bashouti ◽  
Barak Akabayov ◽  
...  

2011 ◽  
Author(s):  
Guoguang Rong ◽  
Shengfei Pan ◽  
Chao Wu ◽  
Xiaobing Li ◽  
Minghong Yang

2014 ◽  
Vol 115 ◽  
pp. 310-316 ◽  
Author(s):  
Nelson Naveas ◽  
Jacobo Hernandez-Montelongo ◽  
Ruth Pulido ◽  
Vicente Torres-Costa ◽  
Raúl Villanueva-Guerrero ◽  
...  

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