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  • 1
    Electronic Resource
    Electronic Resource
    Carrier polymers for cisplatin-type anticancer drug modelsPaper presented at PAT '95, 11-15 June 1995, Pisa, Italy. (1996)
    New York, NY : Wiley-Blackwell
    Polymers for Advanced Technologies 7 (1996), S. 867-872 
    Details
    ISSN: 1042-7147
    Keywords: polymeric drug carriers ; water solubility ; oligo(ethylene oxide) segments ; cis-diaminedichloroplatinum(II) conjugates ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Following a brief discussion of the concept of polymer-drug conjugation and the use of platinum drugs in cancer therapy, the paper presents recent results in the synthesis of water-soluble polymeric carriers designed for the binding of antineoplastic coordination compounds of the cisplatin type. The target polymers, specifically, are linear aliphatic polyamides comprising the ethylenediamine ligand system in the main chain as the potential metal binding site. With solubility in aqueous media a key requirement for intravenously injectable conjugates, the polymers also contain hydrosolubilizing oligo(ethylene oxide) units in the chain, which serve the additional purpose of imparting resistance to serum protein binding and capture by the reticuloendothelial system. The synthesis methods include interfacial polymerization, high-temperature solution polycondensation in polyphosphoric acid and Michael addition polymerization, with 1,2-bis(2-aminoethylamino)ethane and 1,2-bis(3-aminopropylamino)ethane used as the amine comonomers providing the ethylenediamine ligand segment. The target polymers, crudely fractionated by dialysis in 25,000 molecular-mass cult-off tubing, are isolated by freeze-drying as water-soluble solids possessing inherent viscosities of 10-20 ml/g. A selected carrier polymer is converted to the corresponding water-soluble cis-diaminedichloroplatinum(II) conjugate by treatment with tetrachloroplatinate(II) anion in aqueous solution.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Synthesis of water-soluble polyamidoamines for biomedical applications. II. Polymers possessing intrachain-type secondary amino groups suitable for side-chain attachment (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 50 (1993), S. 393-401 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: As part of a program to synthesize water-soluble polymeric carriers suitable for drug binding, the polyaddition reaction of methylenebisacrylamide with comonomers containing two pri-mary amino groups is investigated. The copolymerization of the bisacrylamide with equi-molar quantities of primary diamines under properly controlled experimental conditions is found to proceed in a linear propagation, giving rise to the formation of polyamides comprising two or more secondary amino groups in the recurring unit. Selected diamine monomers include ethylenediamine, diethylenetriamine, triethylenetetramine, 1,2-bis (3-aminopropylamino) ethane, and three 0,0´-bis-(2-aminopropyl) derivatives of poly(ethylene glycol) of different chain length, the last three monomers being chosen because of their outstanding hydrosolubilizing properties. Use of two different diamines in the proper stoi-chiometry leads to corresponding copolymers. The reactions are conducted in aqueous phase over periods of 1-3 days at 65°C, and the polymeric products, possessing the linear polyamidoamine structures 1 and 2, are fractionated by dialysis in membrane tubing with 12000-14000 molecular-mass cutoff and are isolated by freeze-drying as solid or resinous materials possessing complete solubility in water. Inherent viscosities are in the range of 8- 40mLg-1. Microanalytical and spectroscopic data confirm the proposed structures. The suitability of the intrachain secondary amine functions for side chain attachment and drug coupling is demonstrated in model reactions involving N-substitution. © 1993 John Wiley & Sons, Inc.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1993.070500303
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  • 3
    Electronic Resource
    Electronic Resource
    A novel method for surface modification to promote cell attachment to hydrophobic substrates (1998)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 40 (1998), S. 511-519 
    Details
    ISSN: 0021-9304
    Keywords: PEO chemistry ; cell adhesion ; model surface ; RGD peptide ; surface modification ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: The ability to study and regulate cell behavior at a biomaterial interface requires strict control over material surface chemistry. Perhaps the greatest challenge to researchers working in this area is preventing the fouling of a given surface due to uncontrolled protein adsorption. This work describes a method for coupling peptides to hydrophobic materials for the purpose of simultaneously preventing nonspecific protein adsorption and controlling cell adhesion. A hexapeptide containing the ubiquitous RGD cell-adhesion motif was coupled to polystyrene (PS) via a polyethylene oxide (PEO) tether in the form of a modified PEO/PPO/PEO triblock copolymer. Triblocks were adsorbed onto PS at a density of 3.3 ± (5.14 × 10-4) mg/m2 (1.4 × 105 ± 2.12 × 101 molecules/μm2), which was determined by isotope 125I labeling. The peptide, GRGDSY, was activated at the N terminus with N-Succinimidyl 3-(2-pyridyldithio) propionate and coupled to immobilized triblocks where the terminal hydroxyls had been converted to sulfhydryl groups. Surface peptide density was measured by amino acid analysis and found to be 1.4 × 104 ± 0.47 × 104 molecules/μm2. PS modified with PEO/PPO/PEO copolymers alone was found to be inert to cell adhesion both in the presence of serum proteins and when exposed to activated RGD peptide. In contrast, PS conjugated with RGD via end-group-activated PEO/PPO/PEO copolymers supported cell adhesion and spreading. The surface coupling scheme reported here should prove valuable for studying cell-ligand interactions under simplified and highly controlled conditions. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res, 40, 511-519, 1998.
    Additional Material: 3 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    Interaction of plasma proteins with heparinized gel particles studied by high-resolution two-dimensional gel electrophoresis (1991)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 25 (1991), S. 423-441 
    Details
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: In order to further the understanding of protein-surface interactions in the coagulation system, we have chosen to study plasma protein adsorption onto heparin immobilized surfaces. Heparin-binding proteins are abundant in plasma: a search of amino acid sequences revealed that many plasma proteins have possible heparin binding sites. Plasma protein adsorption to the heparinized surfaces is monitored by a novel technique in which the solution depletion of proteins is analytically determined using quantitative two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). This method enables simultaneous, quantitative detection of the majority of plasma proteins before, during, and after their adsorption onto high surface area adsorbents. Using computerized densitometry of silverstained 2-D PAGE gels, the amount of each protein can be determined from the integrated optical density of each protein “spot.” Kinetics of adsorption and adsorption isotherms of four important heparin binding proteins, antithrombin III (ATIII), complement factor C3 (C3), apolipoprotein AI (Apo-AI) and apolipoprotein AIV (Apo-AIV) are reported in this paper. From the adsorption isotherms, the apparent binding constants of each protein-immobilized heparin complex, Ka, were calculated. The surface binding constants were of the same order of magnitude as the respective solution binding constants in the literature. The surface binding constants followed the same order as the respective solution binding constants: Ka (ATIII) 〉 Ka (Apo-AIV) 〉 Ka (C3) 〉 Ka (Apo-AI), indicating that protein binding to the immobilized heparin used is not essentially different from solution binding.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jbm.820250402
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  • 5
    Electronic Resource
    Electronic Resource
    Characterization of soluble polyelectrolyte-gelatin complexes by differential size-exclusion chromatography and flow field-flow fractionation (1998)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part B: Polymer Physics 36 (1998), S. 537-542 
    Details
    ISSN: 0887-6266
    Keywords: sulfonated polyelectrolytes ; gelatin ; complex stoichiometry ; size-exclusion chromatography ; flow field-flow fractionation ; hydrodynamic size ; Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: No abstract.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    NMR three-dimensional solution structure of the serine protease inhibitor cyclotheonamide A (1997)
    New York : Wiley-Blackwell
    Biopolymers 41 (1997), S. 349-358 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The nmr solution conformation of cyclotheonamide A (CtA) was determined in aqueous media. The data produced 15 distance and 10 torsional constraints which were used to generate conformations using restrained simulated annealing (SA) and distance geometry/simulated annealing (DG/SA) calculations. Two different calculation protocols were performed to ensure proper sampling of conformational space and even though the torsional restraints were input differently, both calculation methods yielded the same conformation of CtA. In the structure calculations, all solutions of the Karplus equation were sampled simultaneously using the restrained SA protocol and large ranges were used for the dihedral restraints in the DG/SA protocol because all solutions to the Karplus equation could not be sampled simultaneously. The solution conformation was also compared to the solid state x-ray conformations of CtA bound to thrombin and trypsin. The conformation of the residues important for active site binding (d-Phe, h-Arg, and Pro) are nearly identical in aqueous solution and solid state with largest differences at the a-Ala and v-Tyr residues. CtA appears to be preordered in structure and does not undergo a significant conformational change upon binding to the enzyme active site. © 1997 John Wiley & Sons, Inc.
    Additional Material: 2 Ill.
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