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)

In the aim of protecting stainless steel surfaces against protein and/or bacterial adhesion, thin films including the glycosidase hen egg white lysozyme (HEWL) and/or the synthetic polymer poly(ethylene glycol) (PEG) were covalently coated onto flat substrates by wet chemical processes. Chemical grafting of both species was carried out by covalent binding to surfaces pretreated by the polyamine poly(ethylene imine) (PEI). Surfaces were characterized at each step of functionalization by means of reflection-absorption infrared spectroscopy by modulation of polarization (PM-RAIRS) and X-ray photoelectron spectroscopy (XPS) to determine the atomic and molecular composition of the interfaces, respectively. Then, the ability of the so-modified surfaces to prevent protein adsorption and bacterial adhesion together with their biocide properties were demonstrated by three local tests employing bovine serum albumin (BSA), and the bacteria Listeria ivanovii and Micrococcus luteus. A new test was implemented to assess the local enzymatic properties of HEWL. Cografting of PEG and HEWL resulted in a surface with both antiadhesion and antibacterial properties.
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PMID:Grafting of lysozyme and/or poly(ethylene glycol) to prevent biofilm growth on stainless steel surfaces. 1916 31

Nonfouling surface coatings are of great interest for the development of advanced biomaterials used in biomedical and marine applications. Therefore, a lot of effort has been made to design new biocompatible materials and to understand the mechanisms of the protein repulsion. This study examines a series of polyglycerol (PG) dendrons modified by alkanethiols for their interactions with biofouling relevant proteins: fibrinogen (Fib), lysozyme (Lys), albumin (Alb), and pepsin (Pep). All polyglycerol dendrons [G1.0]-[G3.0] self-assembled monolayers with different terminal functionality (-OH, -OCH(3)) were prepared by applying simple Williamson ether formation followed by radical thiol addition to the alkene. Surface modification was performed by chemisorption of the different dendritic PG derivatives onto gold chips from ethanolic solution and then directly used in a screening with the respective proteins applying SPR spectroscopy. The effective and time-dependent SAM formation on gold was also revealed by X-ray photoelectron spectroscopy. It was demonstrated that the all polyglycerol dendrons [G1.0]-[G3.0] possess excellent resistance to the test proteins. Surprisingly, the SAMs of easily accessible [G1.0] dendron (M(w) = 426 g/mol) modified alkanethiol show the same high protein resistance as we could achieved for high molecular weight polymers (e.g., hyperbranched PG with M(n) = 2500 g/mol). However, significant changes in the amount of adsorbed proteins within the studied time frame of 24 h was not observed. Therefore, these oligoglycerol dendrons are a good alternative for the commonly used poly(ethylene glycol) (PEG).
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PMID:Synthesis and characterization of glycerol dendrons, self-assembled monolayers on gold: a detailed study of their protein resistance. 1935 Nov 58

Segmented polyurethanes (PUs) containing poly(ethylene glycol) (PEG), poly(propylene glycol), or poly(dimethylsiloxane) soft segments have been prepared by two-step condensation polymerization. Atom force microscopy observation in air and solution indicates that the segmented PU forms a microphase separation on the surface. By use of quartz crystal microbalance with dissipation and surface plasmon resonance, we have investigated the adsorption of fibrinogen, bovine serum albumin, and lysozyme on a surface constructed by such a PU in aqueous solution in real time. Our results reveal that the protein resistance of the PUs arises from the hydrated PEG segments instead of microphase separation.
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PMID:Effect of microphase separation on the protein resistance of a polymeric surface. 1937 Oct 47

Proteins have evolved to acquire highly specialized biological functions and are ideal for various applications in both medicine and biotechnology, although denaturation is one of the major problems in protein chemistry. Here, we show a novel strategy for the regulation and preservation of the enzymatic activity even after heat treatment by the complex formation with a cationic smart copolymer, poly(N,N-diethylaminoethyl methacrylate)-graft-poly(ethylene glycol) (PEAMA-g-PEG). PEAMA-g-PEG suppressed the enzymatic activity of lysozyme completely without any conformational change, indicating complex formation and the capping of the active site of lysozyme by PEAMA-g-PEG. The addition of an anionic polymer, poly(acrylic acid) (PAAc), recovered the inhibited enzymatic activity of the lysozyme/PEAMA-g-PEG complex completely. Surprisingly, even after heating the lysozyme with PEAMA-g-PEG for 20 min at 98 degrees C, the addition of PAAc recovered 80% enzymatic activity of lysozyme. Circular dichroism (CD) spectral analysis clearly indicated that the irreversible inactivation of lysozyme induced by the heat treatment was suppressed by the complex formation with PEAMA-g-PEG.
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PMID:Regulation of lysozyme activity based on thermotolerant protein/smart polymer complex formation. 1937 97

A facile method to obtain a thermoreversible physical hydrogel was found by simply mixing an aqueous sol of a block copolymer with a precipitate of a similar copolymer but with a different block ratio. Two ABA-type triblock copolymers poly(D,L-lactic acid-co-glycolic acid)-B-poly(ethylene glycol)-B-poly(D,L-lactic acid-co-glycolic acid) (PLGA-PEG-PLGA) were synthesized. One sample in water was a sol in a broad temperature region, while the other in water was just a precipitate. The mixture of these two samples with a certain mix ratio underwent, however, a sol-to-gel-to-precipitate transition upon an increase of temperature. A dramatic tuning of the sol-gel transition temperature was conveniently achieved by merely varying mix ratio, even in the case of a similar molecular weight. Our study indicates that the balance of hydrophobicity and hydrophilicity within this sort of amphiphilic copolymers is critical to the inverse thermal gelation in water resulting from aggregation of micelles. The availability of encapsulation and sustained release of lysozyme, a model protein by the thermogelling systems was confirmed. This "mix" method provides a very convenient approach to design injectable thermogelling biomaterials with a broad adjustable window, and the novel copolymer mixture platform is potentially used in drug delivery and other biomedical applications.
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PMID:Mixing a sol and a precipitate of block copolymers with different block ratios leads to an injectable hydrogel. 1938 49

Nonspecific adsorption of proteins is a crucial problem in the detection of analytes in complex biological media by affinity sensors operating with label-free detection. We modified the gold surface of surface plasmon resonance (SPR) sensors with three types of promising antifouling coatings: self-assembled monolayers (SAM)s of alkanethiolates terminated with diethylene glycol and carboxylic groups, poly(ethylene glycol) (PEG) grafted onto the SAMs, and zwitterionic polymer brushes of poly(carboxybetaine methacrylate), poly(sulfobetaine methacrylate), and poly(phosphorylcholine methacrylate). Using SPR, we compared the efficacy of the coatings to reduce nonspecific adsorption from human blood plasma and from single-protein solutions of human serum albumin, immunoglobulin G, fibrinogen, and lysozyme. There was no direct relationship between values of water contact angles and plasma deposition on the coated surfaces. A rather high plasma deposition on SAMs was decreased by grafting PEG chains. Fouling on PEG was observed only from plasma fractions containing proteins with molecular mass higher than 350 000 Da. The adsorption kinetics from plasma collected from different healthy donors differed. Poly(carboxybetaine methacrylate) completely prevented the deposition from plasma, but the other more hydrophilic zwitterionic polymers prevented single-protein adsorption but did not prevent plasma deposition. The results suggest that neither wettability nor adsorption of the main plasma proteins was the main indicator of deposition from blood plasma.
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PMID:Interaction of blood plasma with antifouling surfaces. 1940 3

Poly(ethylene glycol) (PEG, MW 2200) chains were introduced into lysozyme molecule. The resulting pegylated lysozyme formed polypseudorotaxanes with alpha- and gamma-cyclodextrins (alpha- and gamma-CyDs, respectively), by inserting one PEG chain in the alpha-CyD cavity and two PEG chains in the gamma-CyD cavity. The pegylated lysozyme/CyD polypseudorotaxanes were less soluble in water and the release rate of the pegylated protein decreased in the order of the pegylated lysozyme>the gamma-CyD polypseudorotaxane>the alpha-CyD polypseudorotaxane. The enzymatic activity of the pegylated lysozyme released from the polypseudorotaxanes was the same as that of the pegylated protein alone, indicating no decrease in the activity through the polypseudorotaxane formation. The results indicate that the pegylated lysozyme/CyD polypseudorotaxanes can work as a slow-release system, and the polypseudorotaxane formation with CyDs may serve as a new strategy for the preparation of slow-release system of pegylated proteins and peptides.
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PMID:Slow-release system of pegylated lysozyme utilizing formation of polypseudorotaxanes with cyclodextrins. 1944 55

In this paper the possibility to tailor degradation and protein release behavior of photopolymerized thermosensitive hydrogels is studied. The hydrogels consist of ABA triblock copolymer, in which the thermosensitive A-blocks are methacrylated poly(N-(2-hydroxypropyl)methacrylamide lactate)s and the B-block is poly(ethylene glycol) with molecular weight of 10 kDa. These hydrogels are prepared by using a combination of physical and chemical cross-linking methods. When a solution of a thermosensitive methacrylated p(HPMAm-lac)-PEG-p(HPMAm-lac) is heated above its cloud point a viscoelastic material is obtained, which can be stabilized by introducing covalent cross-links by photopolymerization. By varying the polymer concentration, hydrogels with different mechanical properties are formed, of which the cross-linking density, mesh size, swelling and degradation behavior can be tuned. It was demonstrated that the release rate of three model proteins (lysozyme, BSA and IgG, with hydrodynamic diameters ranging from 4.1 to 10.7 nm) depended on the protein size and hydrogel molecular weight between cross-links and was governed by the Fickian diffusion. Importantly, the encapsulated proteins were quantitatively released and the secondary structure and the enzymatic activity of lysozyme were fully preserved demonstrating the protein friendly nature of the studied delivery system.
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PMID:Photopolymerized thermosensitive hydrogels for tailorable diffusion-controlled protein delivery. 1952 57

Degradable hydrogels have been extensively used in biomedical applications such as drug delivery, and recent interest has grown in hydrogels that degrade in recognition of a cellular response. This contribution describes a poly(ethylene glycol) (PEG) hydrogel platform with human neutrophil elastase (HNE) sensitive peptide cross-links formed using thiol-ene photopolymerization rendering the gel degradable at sites of inflammation. Further, protein therapeutics can be physically entrapped within the network and selectively released upon exposure to HNE. HNE-responsive hydrogels exhibited surface erosion where the degradation kinetics was influenced by changes in peptide k(cat), concentration of HNE, and concentration of peptide within the gel. Using this platform, we were able to achieve controlled, zero-order release of bovine serum albumin (BSA) in the presence of HNE, and release was arrested in the absence of HNE. To further exploit the advantages of surface eroding delivery systems, a smaller protein (carbonic anhydrase) was delivered at the same rate as BSA and only dependent on gel formulation and environmental conditions. Also, protein release was predicted from a 3-layered hydrogel device using mass loss data. Lastly, the bioactivity of lysozyme was maintained above 90% following the exposure to thiol-ene photopolymerization conditions.
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PMID:Poly(ethylene glycol) hydrogels formed by thiol-ene photopolymerization for enzyme-responsive protein delivery. 1967 84

We measured the viscosity of poly(ethylene glycol) (PEG 6000, 12,000, 20,000) in water using capillary electrophoresis and fluorescence correlation spectroscopy with nanoscopic probes of different diameters (from 1.7 to 114 nm). For a probe of diameter smaller than the radius of gyration of PEG (e.g. rhodamine B or lyzozyme) the measured nanoviscosity was orders of magnitude smaller than the macroviscosity. For sizes equal to (or larger than) the polymer radius of gyration, macroscopic value of viscosity was measured. A mathematical relation for macro and nanoviscosity was found as a function of PEG radius of gyration, R(g), correlation length in semi-dilute solution, xi, and probe size, R. For R < R(g), the nanoviscosity (normalized by water viscosity) is given by exp(b(R/xi)a), and for R > R(g), both nano and macroviscosity follow the same curve, exp(b(R/xi)a), where a and b are two constants close to unity. This mathematical relation was shown to equally well describe rhodamine (of size 1.7 nm) in PEG 20,000 and the macroviscosity of PEG 8,000,000, whose radius of gyration exceeds 200 nm. Additionally, for the smallest probes (rhodamine B and lysozyme) we have verified, using capillary electrophoresis and fluorescence correlation spectroscopy, that the Stokes-Einstein (SE) relation holds, providing that we use a size-dependent viscosity in the formula. The SE relation is correct even in PEG solutions of very high viscosity (three orders of magnitude larger than that of water).
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PMID:Scaling form of viscosity at all length-scales in poly(ethylene glycol) solutions studied by fluorescence correlation spectroscopy and capillary electrophoresis. 1981 21


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