Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hexagonally patterned lysozyme nanoarrays have been assembled on silicon wafers by combining nanosphere lithography and surface silane chemistry using vapor and solution deposition processes. The patterned protein regions extend over cm sized regions, and the size of each island is approximately 120 nm for the solution-prepared template and approximately 60 nm for the vapor-prepared template. Antibody test indicates that the patterned lysozyme maintains its bioactivity on the surface. This new approach offers a fast and reliable method to fabricate protein arrays over large areas with feature sizes comparable to scanning-probe based techniques.
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PMID:Large-scale fabrication of protein nanoarrays based on nanosphere lithography. 1617 62

Silica particles of different porosity were functionalised with iminodiacetic acid (IDA) and loaded with Cu(II) ions to yield Cu(II)-IDA-silica. These immobilised metal affinity chromatography (IMAC) materials were subjected to a comprehensive characterisation study. The Cu(II) content--determined via UV/Vis spectroscopy and atomic absorption spectroscopy (AAS)--was found to be linearly dependent on the specific surface area of the silica particles. The evaluation of protein adsorption isotherms provided information on binding properties towards biomolecules. The data fitted Langmuir's adsorption theory. Binding capacity of hen egg white lysozyme (HEWL) was highest for Cu(II)-IDA-silica with mean pore diameter of 120 A, reaching nearly 350 mg/g. All derivatised materials were applied to the fractionation of human serum samples and subsequent mass spectrometric analysis (m/z: 2000-10,000) according to a surface-enhanced affinity capture (SEAC) protocol. Pore size of the support material affected the appearance of the mass spectra to a great extent, showing that surface morphology is another parameter that has to be considered in addition to surface chemistry. Signal intensity as well as the number of detected masses were strongly dependent on the pore diameter, indicating that the carrier material has to be carefully chosen to assure best results.
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PMID:Cu(II)-loaded iminodiacetic acid-silica particles for protein profiling of human serum samples using surface-enhanced affinity capture: support porosity effects. 1625 43

Lysozyme crystal growth has been localized at the tip of a conventional silicon nitride cantilever through seeded nucleation. After cross-linking with glutaraldehyde, lysozyme protein crystal tips image gold nanoparticles and grating standards with a resolution comparable to that of conventional tips. Force spectra between the lysozyme crystal tips and surfaces covered with antilysozyme reveal an adhesion force that drops significantly upon blocking with free lysozyme, thus confirming that lysozyme crystal tips can detect molecular recognition interactions.
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PMID:Protein crystals as scanned probes for recognition atomic force microscopy. 1635 Nov 89

Speed and accuracy are crucial prerequisites in the application of proteomic methods to clinical medicine. We describe a microfluidic-based nanovial array for rapid proteolytic processing linked to MALDI-TOF MS. This microscale format consumes only minute amounts of sample, and it is compatible with rapid bioanalytical protocols and high-sensitivity readouts. Arrays of vials (300 microm in diameter and 25 microm deep), isotropically etched in silicon wafers were electrochemically porosified. Automated picoliter microdispensing was employed for precise fluid handling in the microarray format. Vials were prefilled with trypsin solution, which was allowed to dry. Porosified and nonporosified nanovials were compared for trypsin digestion and subsequent MS identification of three model proteins: lysozyme, alcohol dehydrogenase, and serum albumin at levels of 100 and 20 fmol. In an effort to assess the rapid digestion platform in a context of putative clinical applications, two prostate cancer biomarkers, prostate-specific antigen (PSA) and human glandular kallikrein 2 (hK2), were digested at levels of 100 fmol (PSA), 20 fmol (PSA) and 8 fmol (hK2). All biomarker digestions were completed in less than 30 s, with successful MS identification in the porous nanovial setting.
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PMID:High-speed biomarker identification utilizing porous silicon nanovial arrays and MALDI-TOF mass spectrometry. 1652 54

A two-dimensionally tunable focusing monochromator has been developed for protein crystallography at high-energy undulator beamlines of third-generation synchrotron radiation facilities. This monochromator consists of a silicon wafer fabricated with an oblique-cut angle between the Bragg net plane and the crystal surface, and adhered onto a table-like copper block. The radii of curvatures are altered independently in two directions by expanding the spaces between the table legs. The versatilities of the meridional and sagittal curvatures were confirmed by X-ray experiments and three-dimensional shape measurements, respectively. The two-dimensional focusing ability was demonstrated using high-energy X-rays of 37.7 keV emitted from a bending-magnet source at the Photon Factory. A quasi-isotropic profile of converged X-rays was achieved near the focal position. The apparent gain of photon flux was 21. As a result of these excellent monochromator characteristics, a diffraction pattern of a hen egg-white lysozyme crystal was successfully obtained using high-energy X-rays.
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PMID:Development of a two-dimensionally tunable focusing monochromator for protein crystallography at high-energy undulator beamlines. 1670 59

The molecular diffusion dynamics in unconstrained cases has been studied thoroughly during the last two centuries, leading to the well-known Fick's diffusion laws and Stokes-Einstein equation. More recently, a new impulse to the study of this topic has been provided by the necessity of understanding the behavior of solute particles in the presence of environmental constraints of size comparable to the molecular dimensions. In this work, we investigate the diffusion kinetics of biomolecules, such as bovine serum albumin, interferon, and lysozyme, through microfabricated silicon membranes, having pores of nanometric size in only one dimension, in the range from few to tens of nanometers (the other dimensions are in the mum range). Experimental results show that the diffusion profiles, in some cases, deviate substantially from those predicted by Fick's laws. In light of these results, a new diffusion mathematical model is proposed, which can reasonably explain the phenomenon and, at the same time, recovers the classical diffusion laws in the unconstrained case. Moreover, a physical description, derived from van der Waals equation of state, is presented, and it is compared with the results obtained by the mathematical model.
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PMID:Dynamic model of biomolecular diffusion through two-dimensional nanochannels. 1685 42

Both end-functionalized (alpha-bromo and omega-carboxy) compounds were first tested for the radical reaction on the silicon-hydride (Si-H) terminated porous silicon (PSi) with/without the presence of diacyl peroxide initiator under microwave irradiation. Then the carboxylic acid monolayers (CAMs) assembled on PSi through the robust Si-C bonds were converted to amino-reactive linker, N-hydroxysuccinimide (NHS)-ester, terminated monolayers. And finally two proteins of bovine serum albumin (BSA) and lysozyme (Lys) were immobilized through amide bonds. The optimum PSi membrane for protein immobilization without collapse, with parameters of porous radii 4-10 nm and depth 0.2-4.6 mum, was prepared from the (100)-oriented p-type silicon wafer. The chemically converted surface products were monitored with Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and field emission scanning electron microscopy (FESEM).
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PMID:Reaction of porous silicon with both end-functionalized organic compounds bearing alpha-bromo and omega-carboxy groups for immobilization of biomolecules. 1685 69

We report in this account our efforts in the development of a novel multiscale simulation tool for integrated nanosystem design, analysis and optimization based on a three-tiered modeling approach consisting of (i) molecular models, (ii) atomistic molecular dynamics simulations, and (iii) dynamical models of protein transport at the continuum scale. In this work we used molecular simulations for the analysis of lysozyme adsorption on a pure silicon surface. The molecular modeling procedures adopted allowed (a) to elucidate the specific mechanisms of interaction between the biopolymer and the silicon surface, and (b) to derive molecular energetic and structural parameters to be employed in the formulation of a mathematical model of diffusion through silicon-based nanochannel membranes, thus filling the existing gap between the nano--and the macroscale.
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PMID:Multiscale modeling of protein transport in silicon membrane nanochannels. Part 1. Derivation of molecular parameters from computer simulations. 1700 64

This study concerns the design of protein-resistant polymer adsorbed layers for the control of surface binding of biospecific recognition entities. Polymer surface layers were prepared using the adsorption of poly(allylamine hydrochloride) (PAH), poly(l-lysine) (PL), and branched and linear polyethyleneimine (PEI) and further modified by the covalent attachment of biotin for specific avidin attachment. The adsorption of PAH, PL, and PEI on silicon substrates was studied as a function of pH and ionic strength using ellipsometry. Average dry layer thicknesses of approximately 10, approximately 5, approximately 9, and approximately 3 A (+/-1 A) were obtained when polymer adsorption occurred from solutions at pH 9.5 that contained 0.5 M NaCl for PAH, PL, branched PEI, and linear PEI, respectively. These polymers showed significant differences in their efficiency to suppress nonspecific avidin adsorption. At low ionic strength, avidin adsorption occurred on all polymer-coated surfaces at basic pH values, despite the same positive electrostatic charge for protein globules and the surface. Though the net electrostatic repulsion between avidin molecules and branched PEI was efficiently screened in a protein solution of pH 7 and 0.15 M NaCl, branched-PEI coatings of high molecular weight were unique in their ability to provide avidin-resistant surfaces as a result of steric hindrance from the branched architecture of adsorbed polymer chains. All polymers studied were effective in suppressing avidin adsorption at pH 3 as a result of protonation of the avidin surface functional groups at this pH. Branched-PEI-coated surfaces were also effective for the suppression of smaller positively charged proteins such as lysozyme and ribonuclease A at pH 7 and 0.15 M NaCl. They were also resistant to the adsorption of negatively charged proteins such as BSA and fibrinogen at pH 7 and 0.75 M NaCl. Furthermore, by using PEI-modified protein-repellent surfaces, selective binding of avidin was achieved to surface-bound silver nanoparticles, which should provide a promising application for the label-free detection of biological species using surface-enhanced Raman scattering (SERS).
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PMID:Control of specific attachment of proteins by adsorption of polymer layers. 1715 22

Fourier transform infrared spectroscopy has been applied to study the thermal stability of multilayer Langmuir-Schaefer (LS) films of lysozyme deposited on silicon substrates. The study has confirmed previous structural findings that the LS protein films have a high thermal stability that is extended in a lysozyme multilayer up to 200 degrees C. 2D infrared analysis has been used here to identify the correlated molecular species during thermal denaturation. Asynchronous 2D spectra have shown that the two components of water, fully and not fully hydrogen bonded, in the high-wavenumber range (2800-3600 cm-1) are negatively correlated with the amine stretching band at 3300 cm-1. On the grounds of the 2D spectra the FTIR spectra have been deconvoluted using three main components, two for water and one for the amine. This analysis has shown that, at the first drying stage, up to 100 degrees C, only the water that is not fully hydrogen bonded is removed. Moreover, the amine intensity band does not change up to 200 degrees C, the temperature at which the structural stability of the multilayer lysozyme films ceases.
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PMID:Thermal stability of lysozyme Langmuir-Schaefer films by FTIR spectroscopy. 1724 Oct 25


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