Synthesis of stable aragonite superstructures by a biomimetic crystallization pathway.
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Calcium Carbonate↗
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Results for “Biomimetics”
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Biomimetic hydrolysis of penicillin G catalyzed by dinuclear zinc(II) complexes: structure-activity correlations in beta-lactamase model systems.
A series of highly preorganized pyrazolate-based dinuclear zinc complexes has been studied as functional synthetic analogues of metallo-beta-lactamases, a class of bacterial enzymes that cause serious clinical problems because of their degradation of common beta-lactam antibiotics. We have investigated the hydrolytic cleavage of penicillin G mediated by the different dinuclear zinc complexes, and have deduced structure-activity correlations. While cooperative effects of the adjacent metal ions might be operative, these are found to either enhance or diminish beta-lactamase activity with respect to a single free zinc. Drastic differences in activity are ascribed to a lack of accessible binding sites after incorporation of the substrate within the bimetallic pocket of 2 and 4, whereas partial detachment of hemilabile ligand side arms in 1 and 3 opens up available coordination sites for nucleophile activation and/or for binding and polarisation of the beta-lactam amide oxygen atom. This interpretation has been corroborated by NMR spectroscopic and mass spectrometric evidence as well as by X-ray crystallography of several adducts formed between the pyrazolate-based dinuclear zinc scaffolds and the small substrate analogue oxazetidinylacetate (oaa), 5-7. In all adducts, the carboxylate group of oaa is the primary anchoring site and is nested in a bridging position within the bimetallic pocket. However, zinc binding of the beta-lactam amide oxygen atom has been confirmed crystallographically for the first time in 7, in which additional open-site coordination sites are available.
Catalysis↗
Modulation of marrow stromal osteoblast adhesion on biomimetic oligo[poly(ethylene glycol) fumarate] hydrogels modified with Arg-Gly-Asp peptides and a poly(ethyleneglycol) spacer.
Novel oligo[poly(ethylene glycol) fumarate] (OPF) hydrogels functionalized with cell adhesion peptides were prepared, and the effects of incorporated peptide density and macromolecular structure of hydrogels on attachment and morphology of marrow stromal cells (MSCs) were evaluated. Poly(ethylene glycol) (PEG; number average molecular weight of 930, 2860, and 6090) was used to synthesize OPF. A model peptide, Gly-Arg-Gly-Asp (GRGD), was incorporated into OPF hydrogels after being coupled to acrylated PEG of molecular weight 3400. The increase of incorporated peptide concentration enhanced MSC attachment to OPF hydrogels of PEG of molecular weight of 930 and 2860. However, the number of attached MSCs to OPF hydrogels of PEG (molecular weight 6090) remained constant regardless of the peptide density. The length of PEG in OPF also influenced cell attachment. When 1 micromole peptide/g hydrogel was incorporated into the OPF hydrogels, the degree of cell attachment at 12 h relative to the initial seeding density was 93.9 +/- 5.9%, 64.7 +/- 8.2%, and 9.3 +/- 6.6% for OPF hydrogels prepared with PEG of molecular weights of 930, 2860, and 6090, respectively. However, the crosslinking density of hydrogels did not significantly affect cell attachment. The interaction was sequence specific, in that MSC attachment to GRGD-modified hydrogels was competitively inhibited when cells were incubated in the presence of 0.5 mM soluble GRGD before cell seeding. These results suggest that we can modulate MSC attachment to OPF hydrogels by altering the peptide density and the molecular structure of OPF hydrogels.
Animals↗
Biomimetic surface modification of poly (L-lactic acid) with gelatin and its effects on articular chondrocytes in vitro.
Our objective in this study was to investigate the efficiency of two treatments for poly (L-lactic acid) (PLLA) surface modification with gelatin, via entrapment and coupling, using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) and N-hydroxysuccinimide (NHS). The properties of original PLLA, gelatin-entrapped, and coupled PLLA films were investigated by water contact angle measurement and electron spectroscopy for chemical analysis (ESCA). The water contact angle indicated that the incorporation of gelatin resulted in a change in hydrophilicity, and the ESCA data suggested that the modified PLLA films became enriched with nitrogen atoms. The cytocompatibility of modified PLLA films might be improved. Therefore, we examined the attachment and proliferation of bovine articular chondrocyte seeded on modified PLLA films and virgin films. A whole-cell enzyme-linked immunosorbent assay (cell ELISA) that detects 5-bromo-2'-deoxyuridine (BrdU) incorporation during DNA synthesis and collagen type II secretion was applied to evaluate the chondrocytes on different PLLA films and tissue culture plates (TCPS). Cell viability was estimated by the MTT [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide] assay, and cell function was assessed by measuring glycosaminoglycan (GAG) secreted by chondrocytes. These results implied that gelatin used to modify the PLLA surface through entrapment and coupling could enhance chondrocyte adhesion, proliferation, and function.
Animals↗
Visualization of specific interaction between biomimetic glycopolymer containing reducing glucose moiety and HepG2 cell mediated by GLUT-1.
Poly [3-O-(4'-vinylbenzyl)-D-glucose] (PVG) is a polystyrene derivative that contains glucose moieties, which interact with glucose transporter (GLUT-1)-carrying HepG2 cells. To clarify the specific interaction between the PVG and HepG2 cells, PVG polymer labeled with fluorescent rhodamine-B isothiocyanate (RITC) was used to follow the specific interaction, which was visualized by confocal laser microscopy. We found that PVG binds strongly to HepG2 cells, probably because of a specific interaction mediated by the presence of GLUT-1 on the cell membrane. The fluorescence intensity of PVG and HepG2 cells was up to fourfold (0.11 +/- 0.04) that of any other glycopolymer and HepG2 cell interaction (0.025 +/- 0.01). Moreover, cellular fluorescence increased significantly on increasing the incubation time and the polymer concentration. To verify the specific nature of the interaction between PVG and HepG2 cells, the cells were pretreated with phloretin, an inhibitor of GLUT-1 before adding RITC-labeled PVG polymer to the cell culture medium; this treatment was found to suppress the action of PVG on HepG2 cells.
Biocompatible Materials↗
Use of a biomimetic strategy to engineer bone.
Engineering trabecular-like, three-dimensional bone tissue throughout biodegradable polymer scaffolds is a significant challenge. Using a novel processing technique, we have created a biodegradable scaffold with geometry similar to that of trabecular bone. When seeded with bone-marrow cells, new bone tissue, the geometry of which reflected that of the scaffold, was evident throughout the scaffold volume and to a depth of 10 mm. Preseeded scaffolds implanted in non-healing rabbit segmental bone defects allowed new functional bone formation and bony union to be achieved throughout the defects within 8 weeks. This marks the first report of successful three-dimensional bone-tissue engineering repair using autologous marrow cells without the use of supplementary growth factors. We attribute our success to the novel scaffold morphology.
Animals↗
Porous Ti-6Al-4V alloy fabricated by spark plasma sintering for biomimetic surface modification.
Porous compacts with both biological and biomechanical compatibilities and high strength were developed. Spherical powders of Ti-6Al-4V alloy, which were either as received or surface modified with the use of calcium ions by hydrothermal treatment (HTT), were fabricated by a spark plasma sintering process. The porous compacts of pure Ti were used as reference materials. Porosity was approximately 30%, and compressive strengths were 113 and 125 MPa for the as-received Ti alloy powders and those modified by the HTT process, respectively. The bending strength and elastic modulus of as-received Ti alloy powders were 128-178 MPa and 16-18 GPa, respectively. Each of the compacts was immersed in simulated body fluid (SBF). The amount of adsorption/precipitation of calcium phosphate through the compacts was measured by weight change and was observed by SEM. The compacts were covered with calcium phosphate after 2 weeks of immersion in SBF. The compacts of Ti alloy had plenty of precipitated apatite crystals, and modification by HTT accumulated more precipitation. Because calcium phosphate is a mineral component of bone, apatite, which is precipitated on the surface of the compacts, could adsorb proteins and/or drugs such as antibiotics. It is expected that a large amount of proteins and/or drugs could be impregnated when the porous compacts developed are used.
Alloys↗
[Key pericyclic reactions in biological systems and biomimetic synthesis--an overview].
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Animals↗
Covalent attachment of functionalized lipid bilayers to planar waveguides for measuring protein binding to biomimetic membranes.
A new method is presented for measuring sensitively the interactions between ligands and their membrane-bound receptors in situ using integrated optics, thus avoiding the need for additional labels. Phospholipid bilayers were attached covalently to waveguides by a novel protocol, which can in principle be used with any glass-like surface. In a first step, phospholipids carrying head-group thiols were covalently immobilized onto SiO2-TiO2 waveguide surfaces. This was accomplished by acylation of aminated waveguides with the heterobifunctional crosslinker N-succinimidyl-3-maleimidopropionate, followed by the formation of thioethers between the surface-grafted maleimides and the synthetic thiolipids. The surface-attached thiolipids served as hydrophobic templates and anchors for the deposition of a complete lipid bilayer either by fusion of lipid vesicles or by lipid self-assembly from mixed lipid/detergent micelles. The step-by-step lipid bilayer formation on the waveguide surface was monitored in situ by an integrated optics technique, allowing the simultaneous determination of optical thickness and one of the two refractive indices of the adsorbed organic layers. Surface coverages of 50-60% were calculated for thiolipid layers. Subsequent deposition of POPC resulted in an overall lipid layer thickness of 45-50 A, which corresponds to the thickness of a fluid bilayer membrane. Specific recognition reactions occurring at cell membrane surfaces were modeled by the incorporation of lipid-anchored receptor molecules into the supported bilayer membranes. (1) The outer POPC layer was doped with biotinylated phosphatidylethanolamine. Subsequent specific binding of streptavidin was optically monitored. (2) A lipopeptide was incorporated in the outer POPC monolayer. Membrane binding of monoclonal antibodies, which were directed against the peptide moiety of the lipopeptide, was optically detected. The specific antibody binding correlated well with the lipopepitde concentration in the outer monolayer.
Acylation↗
Use of a biomimetic peptide in the design of a competitive binding assay for biotin and biotin analogues.
A competitive binding assay for biotin, biocytin, and desthiobiotin utilizing a genetically engineered enzyme-ligand conjugate is described herein. This assay is unique in that the enzyme-ligand conjugate consists of the streptavidin binding peptide Strep-tag II, which mimics the binding of biotin to streptavidin, rather than biotin itself. This allows for the construction of a well-defined, oligosubstituted enzyme-ligand conjugate for which the site of attachment of the ligand on the enzyme is known precisely. The assay has detection limits of 5 x 10(-8) M for biotin, 1 x 10(-7) M for biocytin, and 2 x 10(-6) M for desthiobiotin, and it serves as a model system in that it demonstrates the feasibility of using enzyme-ligand conjugates in which a peptide mimic of the analyte ligand is genetically fused to the enzyme. This avoids the problems associated with covalent attachment of the ligand to the enzyme, such as multiple substitution of the ligand and variability of the site of attachment. To our knowledge, this is the first example of using an enzyme-peptide mimic conjugate to detect a nonpeptide analyte.
Amino Acid Sequence↗
Biomimetic chemistry in Japan.
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Enzymes↗
Chiral linear hydroxamates as biomimetic analogues of ferrioxamine and coprogen and their use in probing siderophore-receptor specificity in bacteria and fungi.
Linear hydroxamate derivatives, possessing chiral alpha-amino acid moieties, were synthesized and their iron transport activities were studied in bacteria and fungi. No growth-promoting activity could be detected in the Gram-positive hydroxamate-auxotroph Aureobacterium flavescens JG9. However, Gram-negative enterobacteria, such as Escherichia coli, Pantoea agglomerans and Hafnia alvei were able to utilize iron from these analogues. Uptake of 55Fe-labeled analogues was inhibited by sodium azide, suggesting an active transport process. The receptors involved during uptake in enterobacteria were identified by using appropriate indicator organisms which are defective in the transport of either ferrioxamines (P. agglomerans FM13), coprogens (H. alvei), or both of these siderophore classes (E. coli fhuE). Our data suggest that the chiral hydroxamates are recognized by the ferrioxamine receptor (FoxA) and the coprogen receptor (FhuE) at a ratio which depends on the optical lambda/delta isomer fraction and the nature of side chains. Transport was also observed in the fungus Neurospora crassa, known to take up coprogen rather than ferrioxamines, suggesting that in this fungus the synthetic analogues behave like coprogen.
Bacteria↗
Simulating arterial wall calcification in vitro: biomimetic crystallization of calcium phosphates under controlled conditions.
OBJECTIVES: A method to simulate the biological and pathological crystallization of calcium phosphate in vitro is presented. BACKGROUND: The pathological crystallization of calcium phosphates during atherosclerosis is still poorly understood as it depends on a variety of external factors, e.g., the presence of biological molecules that act as crystallization promoters or inhibitors. METHODS: A computer-controlled double-diffusion device is presented that permits crystallization under constant external conditions (constant pH, constant concentrations of Ca2+ and PO4(3-)). RESULTS: The crystallization of hydroxyapatite occurs in a well-defined way. The presence of additives (cholesterol, magnesium) distinctively alters the morphology of the crystals. CONCLUSIONS: The simulation of pathological crystallization as in atherosclerosis is possible if the external conditions are kept strictly constant during the experiment. In order to obtain a meaningful insight into biological crystallization, this approach is essential as otherwise the external conditions change continuously during the experiment. The effect of additives can be conveniently studied.
Arteriosclerosis↗
A biomimetic electron releasing device: capacitively connected glow discharge electrode.
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Electrochemistry↗
Will biomimetics provide new answers for old problems of calcified tissues?
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Animals↗
Binding of nitrite and its reductive activation to nitric oxide at biomimetic copper centers.
The reactivity of nitrite towards the copper(II) and copper(I) centers of a series of complexes with tridentate nitrogen donor ligands has been investigated. The ligands are bis[(1-methylbenzimidazol-2-yl)methyl]amine (1-bb), bis[2-(1-methylbenzimidazol-2-yl)ethyl]amine (2-bb), and bis[2-(3,5-dimethyl-1-pyrazolyl)ethyl]amine (ddah) and carry two terminal benzimidazole (1-bb, 2-bb) or pyrazole (ddah) rings and a central amine donor residue. While 2-bb and ddah form two adjacent six-membered chelate rings on metal coordination, 1-bb forms two smaller rings of five members. The binding affinity of nitrite and azide to the Cu(II) complexes (ClO4- as counterion) has been determined in solution. The association constants for the two ligands are similar, but nitrite is a slightly stronger ligand than azide when it binds as a bidentate donor. The X-ray crystal structure of the nitrite complex [Cu(ddah)(NO2)]ClO4 (final R=0.056) has been determined: triclinic P1space group, a=8.200(2) A, b=9.582(3) A, c=15.541(4) A. It may be described as a perchlorate salt of a "supramolecular" species resulting from the assembly of two complex cations and one sodium perchlorate unit. The copper stereochemistry in the complex is intermediate between SPY and TBP, and nitrite binds to Cu(II) asymmetrically, with Cu-O distances of 2.037(2) and 2.390(3) A and a nearly planar CuO2N cycle. On standing, solutions of [Cu(ddah)(NO2)]ClO4 in methanol produce the dinuclear complex [Cu(ddah)(OMe)]2(ClO4)2, containing dibridging methoxy groups. In fact the crystal structure analysis (final R=0.083) showed that the crystals are built up by dinuclear cations, arranged on a crystallographic symmetry center, and perchlorate anions. Electrochemical analysis shows that binding of nitrite to the Cu(II) complexes of 2-bb and ddah shifts the reduction potential of the Cu(II)/Cu(I) couple towards negative values by about 0.3 V. The thermodynamic parameters of the Cu(II)/Cu(I) electron transfer have also been analyzed. The mechanism of reductive activation of nitrite to nitric oxide by the Cu(I) complexes of 1-bb, 2-bb, and ddah has been studied. The reaction requires two protons per molecule of nitrite and Cu(I). Kinetic experiments show that the reaction is first order in [Cu(I)] and [H+] and exhibits saturation behavior with respect to nitrite concentration. The kinetic data show that [Cu(2-bb)]+ is more efficient than [Cu(1-bb)]+ and [Cu(ddah)]+ in reducing nitrite.
Anaerobiosis↗
Inhibition of the catecholase activity of biomimetic dinuclear copper complexes by kojic acid.
The inhibition of the catechol oxidase activity exhibited by three dinuclear copper(II) complexes, derived from different diaminotetrabenzimidazole ligands, by kojic acid [5-hydroxy-2-(hydroxymethyl)-gamma-pyrone] has been studied. The catalytic mechanism of the catecholase reaction proceeds in two steps and for both of these inhibition by kojic acid is of competitive type. The inhibitor binds strongly to the dicopper(II) complex in the first step and to the dicopper-dioxygen adduct in the second step, preventing in both cases the binding of the catechol substrate. Binding studies of kojic acid to the dinuclear copper(II) complexes and a series of mononuclear analogs, carried out spectrophotometrically and by NMR, enable us to propose that the inhibitor acts as a bridging ligand between the metal centers in the dicopper(II) catalysts.
Algorithms↗
Biomimetic approach to the oxygen evolving center: resonance Raman investigation of a manganese mu-oxo dimer in three oxidation states.
A biologically relevant dinuclear manganese mono-mu-oxo complex with a bound phenolate ligand in three oxidation states, (III,III), (III,IV) and (IV,IV), was studied using resonance Raman spectroscopy. Depending upon the excitation frequency, phenolate vibrations or mu-oxo vibrations were enhanced, which allowed us to assign the UV-visible absorption spectra. In the case of the mixed valence species (III,IV), the mu-oxo vibration at 854 cm-1 has been assigned by isotopic substitution (H2(18)O) to nu as(Mn-O-Mn). This preferential enhancement of the asymmetric vibration stresses the asymmetric character of the bridge.
Dimerization↗