Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The preparation of a stable affinity medium with heparin as the affinity ligand has been investigated. Glyceryl controlled-pore glass (CPG) was activated with 1-cyano-4-dimethylaminopyridinium tetrafluoroborate and coupled with heparin. This affinity medium was used to separate some simple proteins, trypsinogen and lysozyme, in a high-performance liquid chromatographic configuration. The heparin-glyceryl-CPG was also used to separate alpha- and beta-lipoproteins in human serum. The effectiveness of the separation is confirmed by radial immunodiffusion and the determination of the cholesterol content of each of the separated fractions.
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PMID:Preparation of heparin-glyceryl controlled-pore glass affinity media for the separation of alpha- and beta-lipoproteins. 156 91

We report a new process of making highly-porous large polymeric microparticles for local drug delivery to the lungs by inhalation. Poly(lactic-co-glycolic acid) (PLGA) microparticles (average diameter, 10-20 microm) were made by the double-emulsion method. To impart favorable aerodynamic properties, an effervescent salt ammonium bicarbonate (ABC) was included in the internal aqueous phase. ABC produced highly-porous structures in the PLGA particles as it escaped as ammonia and carbon dioxide. The fine-particle fraction (FPF) of the microparticles increased as a function of the ratio of ABC to PLGA. Microparticles prepared with 7.5%w/w (ABC/PLGA) had a mass median aerodynamic diameter (MMAD) of 4.0 +/- 1.2 microm and FPF of 32.0 +/- 9.1% when tested with Anderson Cascade Impactor (ACI) and Rotahaler. The highly-porous large particles deposited at the ACI stages corresponding to the trachea and below. The highly-porous large particles avoided phagocytosis by macrophages, while non-porous small particles were quickly taken up by the macrophages. Unlike other encapsulation methods which employ osmogens or extractable porogens, this method could encapsulate lysozyme and doxorubicin.HCl, with high encapsulation efficiency ( approximately 100% for both lysozyme and doxorubicin), in the PLGA microparticles characterized by desirable MMAD (4.5 +/- 0.6 microm lysozyme; 4.6 +/- 0.4 microm doxorubicin) and FPF (29.1 +/- 12.2% lysozyme; 33.8+/-3.6% doxorubicin). Fifty-two percent of encapsulated doxorubicin was released over 4 days from the highly-porous microparticles. This method is an efficient way of making polymeric microparticles for sustained local drug delivery by inhalation.
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PMID:Development of highly porous large PLGA microparticles for pulmonary drug delivery. 1913 45

Parallel Cascade Selection Molecular Dynamics (PaCS-MD) is proposed as a molecular simulation method to generate conformational transition pathway under the condition that a set of "reactant" and "product" structures is known a priori. In PaCS-MD, the cycle of short multiple independent molecular dynamics simulations and selection of the structures close to the product structure for the next cycle are repeated until the simulated structures move sufficiently close to the product. Folding of 10-residue mini-protein chignolin from the extended to native structures and open-close conformational transition of T4 lysozyme were investigated by PaCS-MD. In both cases, tens of cycles of 100-ps MD were sufficient to reach the product structures, indicating the efficient generation of conformational transition pathway in PaCS-MD with a series of conventional MD without additional external biases. Using the snapshots along the pathway as the initial coordinates, free energy landscapes were calculated by the combination with multiple independent umbrella samplings to statistically elucidate the conformational transition pathways.
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PMID:Parallel Cascade Selection Molecular Dynamics (PaCS-MD) to generate conformational transition pathway. 2388 57

Parallel Cascade Selection Molecular Dynamics (PaCS-MD) is an efficient conformational sampling method for generating a set of reactive trajectories that connect a given reactant and a product. In PaCS-MD, initial structures relevant to conformational transitions are reasonably selected by referring to a set of reaction coordinates (RCs), and short-time molecular dynamics (MD) simulations are independently launched from them. To efficiently perform PaCS-MD, specifications of RCs are essential, but specifying reasonable RCs is generally nontrivial. In the present study, we propose on-the-fly specifications of RCs as an extended PaCS-MD. In the present method, n types of RCs are provided as candidates a priori as follows: RC = (X1, X2, ..., X n), and one of the RCs is specified in a cycle-dependent manner, i.e. the reasonable RC is searched at every cycle by evaluating gradients of the RCs, i.e. RC with the steepest gradient for cycle is regarded as the reasonable RC, and conformational resampling proceeds along it, promoting conformational transition of a given protein. For a demonstration, the extended PaCS-MD was applied to reproduce the open-closed conformational transition of T4 lysozyme (T4L). As candidates of possible RCs, (1) root-mean square distance, (2) principal coordinates, (3) accessible surface area, (4) radius of gyration, and (5) end-to-end distance were adopted in the cycle-dependent specifications of RCs. Through the demonstration, the extended PaCS-MD successfully reproduced the conformational transition from the open to closed states of T4L. As a more complicated practice, a dimerization process of diubiquitin was efficiently reproduced with the extended PaCS-MD, showing the high conformational sampling efficiency of the present algorithm. In contrast, the conventional PaCS-MD with a fixed RC sometimes failed to generate a set of reactive trajectories when an unreasonable RC was specified, i.e. the conformational sampling efficiency of PaCS-MD might more or less depend on the specified RCs. Judging from the present demonstrations, on-the-fly specifications of RCs might be effective in reproducing/predicting essential transitions of a given protein.
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PMID:On-the-Fly Specifications of Reaction Coordinates in Parallel Cascade Selection Molecular Dynamics Accelerate Conformational Transitions of Proteins. 2972 81