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  • 1995-1999  (21)
  • 1965-1969  (5)
  • Chemistry  (24)
  • Caco-2 cells  (2)
  • 1
    Electronic Resource
    Electronic Resource
    The Effect of β-Turn Structure on the Passive Diffusion of Peptides Across Caco-2 Cell Monolayers (1997)
    Springer
    Pharmaceutical research 14 (1997), S. 1332-1340 
    Details
    ISSN: 1573-904X
    Keywords: peptide delivery ; paracellular diffusion ; transcellular diffusion ; solution conformation ; Caco-2 cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. To investigate the relationships between the β-turn structure of a peptide and its passive diffusion across Caco-2 cell monolayers, an in vitro model of the intestinal mucosa. Methods. Linear hydrophilic peptides (Ac-TyrProXaaZaaVal-NH2; Xaa = Gly, Ile and Zaa = Asp, Asn) and hydrophobic (Ac-YaaPro-XaaIleVal-NH2; Yaa = Tyr, Phe and Xaa = Gly, Ile: and Ac-PhePro-XaaIle-NH2; Xaa = Gly, He) peptides were synthesized and their effective permeability coefficients (Peff) were determined across Caco-2 cell monolayers. The lipophilicities of the peptides were estimated by measuring their partition coefficients (Po/w) between 1-octanol and HBSS. Two-dimensional NMR (2D-NMR) spectroscopy and circular dichroism (CD) spectroscopy was used to determine the solution structures of these model peptides. Results. Using 2D-NMR spectroscopy and CD spectroscopy, the hydrophilic Gly-containing peptides (Ac-TyrProGlyZaaVal-NH2; Zaa = Asp, Asn) were shown to exhibit a higher degree of β-turn structure in solution than the Ile-containing peptides (Ac-TyrProIleZaaVal-NH2; Zaa = Asp, Asn). CD spectroscopy was used to show that the Gly-containing hydrophobic peptides (Ac-YaaProGlyIleVal-NH2; Yaa = Tyr, Phe: and Ac-PheProGlyIle-NH2) exhibited a higher degree of β-turn structure in solution than the Ile-containing hydrophobic peptides. The Peff values of all four hydrophilic peptides across unperturbed Caco-2 cell monolayers were very low and no statistically significant differences were observed between the Gly- and Ile-containing penta-peptides within either the Asp or Asn series. The Peff values for the hydrophobic Gly-containing peptides were significantly greater than the Peff values determined for their Ile-containing counterparts. The Gly-containing penta- and tetrapeptides in the Phe series, which exhibited high permeation, were shown to be metabolically unstable. In contrast, the Gly- and Ile-containing pentapeptides in the Tyr series and the Ile-containing penta- and tetrapeptides in the Phe series, which exhibited low permeation, were metabolically stable. Conclusions. Hydrophobic peptides that exhibit significant β-turn structure in solution are more lipophilic as measured by log Po/w and more readily permeate Caco-2 cell monolayers via the transcellular route than hydrophobic peptides that lack this type of solution structure. The ability of these peptides to permeate Caco-2 cell monolayers via the transcellular route also exposed them to metabolism, presumably by cytosolic endopeptidases. Similar secondary structural features in hydrophilic peptides do not appear to sufficiently alter the physicochemical properties fo the peptides so as to alter their paracellular flux through unperturbed Caco-2 cell monolayers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1012152117703
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of Restricted Conformational Flexibility on the Permeation of Model Hexapeptides Across Caco-2 Cell Monolayers (1997)
    Springer
    Pharmaceutical research 14 (1997), S. 169-175 
    Details
    ISSN: 1573-904X
    Keywords: peptide delivery ; conformation ; Caco-2 cells ; membrane permeability ; NMR ; CD
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. To determine how restricted conformational flexibility of hexapeptides influences their cellular permeation characteristics. Methods. Linear (Ac-Trp-Ala-Gly-Gly-X-Ala-NH2; X = Asp, Asn, Lys) and cyclic (cyclo[Trp-Ala-Gly-Gly-X-Ala]; X = Asp, Asn, Lys) hexapeptides were synthesized, and their transport characteristics were assessed using the Caco-2 cell culture model. The lipophilicities of the hexapeptides were determined using an immobilized artificial membrane. Diffusion coefficients used to calculate molecular radii were determined by NMR. Two-dimensional NMR spectroscopy, circular dichroism, and molecular dynamic simulations were used to elucidate the most favorable solution structure of the cyclic Asp-containing peptide. Results. The cyclic hexapeptides used in this study were 2−3 times more able to permeate (e.g., Papp = 9.3 ± 0.3 × 10−8 cm/sec, X = Asp) the Caco-2 cell monolayer than were their linear analogs (e.g., Papp = 3.2 ± 0.3 × 10−8 cm/sec, X = Asp). In contrast to the linear hexapeptides, the flux of the cyclic hexapeptides was independent of charge. The cyclic hexapeptides were shown to be more lipophilic than the linear hexapeptides as determined by their retention times on an immobilized phospholipid column. Determination of molecular radii by two different techniques suggests little or no difference in size between the linear and cyclic hexapeptides. Spectroscopic data indicate that the Asp-containing linear hexapeptide exists in a dynamic equilibrium between random coil and β-turn structures while the cyclic Asp-containing hexapeptide exists in a well-defined compact amphophilic structure containing two β-turns. Conclusions. Cyclization of the linear hexapeptides increased their lipophilicities. The increased permeation characteristics of the cyclic hexapeptides as compared to their linear analogs appears to be due to an increase in their flux via the transcellular route because of these increased lipophilicities. Structural analyses of the cyclic Asp-containing hexapeptide suggest that its well-defined solution structure and, specifically the existence of two β-turns, explain its greater lipophilicity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1012092409216
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  • 3
    Electronic Resource
    Electronic Resource
    Structural investigation of C4b-binding protein by molecular modeling: Localization of putative binding sites (1998)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 31 (1998), S. 391-405 
    Details
    ISSN: 0887-3585
    Keywords: complement control protein ; protein modeling ; blood coagulation ; C4b-binding protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: C4b-binding protein (C4BP) contributes to the regulation of the classical pathway of the complement system and plays an important role in blood coagulation. The main human C4BP isoform is composed of one β-chain and seven α-chains essentially built from three and eight complement control protein (CCP) modules, respectively, followed by a nonrepeat carboxy-terminal region involved in polymerization of the chains. C4BP is known to interact with heparin, C4b, complement factor I, serum amyloid P component, streptococcal Arp and Sir proteins, and factor VIII/VIIIa via its α-chains and with protein S through its β-chain. The principal aim of the present study was to localize regions of C4BP involved in the interaction with C4b, Arp, and heparin. For this purpose, a computer model of the 8 CCP modules of C4BP α-chain was constructed, taking into account data from previous electron microscopy (EM) studies. This structure was investigated in the context of known and/or new experimental data. Analysis of the α-chain model, together with monoclonal antibody studies and heparin binding experiments, suggests that a patch of positively charged residues, at the interface between the first and second CCP modules, plays an important role in the interaction between C4BP and C4b/Arp/Sir/heparin. Putative binding sites, secondary-structure prediction for the central core, and an overall reevaluation of the size of the C4BP molecule are also presented. An understanding of these intermolecular interactions should contribute to the rational design of potential therapeutic agents aiming at interfering specifically some of these protein-protein interactions. Proteins 31:391-405, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Sucrose diacrylate: A unique chemically and biologically degradable crosslinker for polymeric hydrogels (1997)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 35 (1997), S. 2221-2229 
    Details
    ISSN: 0887-624X
    Keywords: biodegradation ; hydrogels ; crosslinking agent ; sucrose diacrylate ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A series of degradable hydrogels based on different vinyl monomers such as acrylamide, sucrose-1′-acrylate, and acrylic acid were synthesized using sucrose-6,1′-diacrylate (SDA) as a crosslinking agent. SDA was prepared by enzymatic transesterification of vinyl acrylate with sucrose in pyridine. Base catalyzed hydrolysis of SDA in aqueous solution was studied as a function of pH. As expected, hydrolysis of SDA was faster at higher pHs such that poly(acrylamide), poly(sucrose 1′-acrylate), and poly(acrylic acid) hydrogels underwent substantial degradation at and above pH 7, 9, and 13, respectively. The degradation was characterized by changes in the swelling ratios of the hydrogels indicating breakage of the crosslinking agent. Degradation of the hydrogels at their chemically stable pHs was studied in presence of enzymes. Enzymes, including pepsin and a fungal Lipase, were able to degrade the poly(acrylamide) hydrogel at pH 4 and 5, respectively. Poly(acrylic acid) hydrogel was degraded in presence of a fungal protease at pH 7.8. © 1997 John Wiley & Sons, Inc. J Polym Sci A: Polym Chem 35: 2221-2229, 1997
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Crystallization of ADP-ribosyl cyclase from Aplysia californica (1996)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 24 (1996), S. 138-140 
    Details
    ISSN: 0887-3585
    Keywords: ADP-ribosyl cyclase ; crystals ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: ADP-ribosyl cyclase synthesizes the secondary messenger cyclic ADP-ribose from NAD+. Diffraction quality crystals of the enzyme from ovotestes of Aplysia californica have been obtained. Crystallographic analysis of this enzyme will yield insight into the mode of binding of the novel cyclic nucleotide and the mechanism by which NAD+ is cyclized.
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    The preparation and characterization of poly(urethane-peo-polar siloxane) complexes as polymer electrolytes (1995)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 33 (1995), S. 2033-2038 
    Details
    ISSN: 0887-624X
    Keywords: ion-conducting polymers ; polar siloxanes ; stability ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A series of novel poly(urethane-PEO-polar siloxane) copolymers and their complexes with LiClO4 were prepared for assessment as polymer electrolytes and characterized by IR, GPC, and DSC, and their ionic conductivity and thermal stability were tested. The incorporation of polar siloxanes into U-PEO greatly increased conductivity. The highest conductivity was 2.6 × 10-5 S cm-1 at 25°C. The correlation between Tg, conductivity, and the ratio of siloxane to PEO as well as stability of the polymers are discussed. © 1995 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pola.1995.080331210
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  • 7
    Electronic Resource
    Electronic Resource
    New polar silane-PEO polyester complexes as polymer electrolytes (1998)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 36 (1998), S. 1093-1106 
    Details
    ISSN: 0887-624X
    Keywords: ion-conducting polymers ; silicon ; synthesis ; stability ; conductivity ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Trifunctional carbosilanes containing hydroxy and cyano groups have been synthesized in good yields and incorporated into polyether-based electrolytes. The new linear and cross-linked modified PEOs have been characterized by DSC and conductivity measurements. The effect of silane content, the length of the PEO block, glycerol concentration, and temperature on glass transition temperature and conductivity of lithium salts complexes of these materials has been evaluated. The new materials showed improved conductivity (∼ 10-5 S cm-1) at ambient temperatures compared with unmodified polyethers. © 1998 John Wiley & Sons, Inc. J Polym Sci A: Polym Chem 36: 1093-1106, 1998
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Protein transport in ultrafiltration hollow-fiber bioreactors (1995)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 41 (1995), S. 415-425 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A 1-D model, which neglects radial variations, describes the hydrodynamics of cell-free ultrafiltration hollow-fiber bioreactors (HFBRs) and the transport of highmolecular-weight proteins trapped in the extracapillary space (ECS). The profiles of radially-averaged protein concentrations predicted by this model are identical to those obtained using a model with radial variations. The model predictions agree well with axial profiles of bovine serum albumin (BSA) and human transferrin concentrations measured in transient and steady-state experiments. The validated model explores the influence of cell culture operating conditions on HFBR protein transport. Increasing protein loading decreases BSA and transferrin polarization in HFBRs operated with unidirectional lumen flow. A relationship developed predicts the protein loading needed to ensure a nonzero steady-state protein concentration throughout the ECS. This critical protein loading depends only on the lumen pressure drop and the ECS protein osmotic pressure. Periodic reversal of the lumen flow direction also decreases protein polarization. The influence of the flow-direction switching time and membrane permeability on the ECS protein distribution is investigated.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690410222
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  • 9
    Electronic Resource
    Electronic Resource
    Mathematical model of mass transport through dispersed-phase polymer networks (1995)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 41 (1995), S. 805-811 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A mathematical model of mass transport through dispersed-phase networks to be used for the sustained release of drugs or other solutes at steady rates is presented. The drug is assumed to be encapsulated within the dispersed microdomains and transported to the bulk by diffusion across the interface. A drug is released to the surroundings by diffusion through the bulk. The results show that the desired steady flux of a drug to the surroundings may be obtained given appropriate values of structural properties of the network. These properties may be manipulated easily in the fabrication of dispersed-phase networks reported previously.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690410407
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  • 10
    Electronic Resource
    Electronic Resource
    Synthesis and analysis of the enantiomers of calmidazolium, and a 1H NMR demonstration of a chiral interaction with calmodulin (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Chirality 8 (1996), S. 545-550 
    Details
    ISSN: 0899-0042
    Keywords: nuclear magnetic resonance ; isotopically labelled proteins ; drug-protein interactions ; chiral interaction ; calmodulin antagonism ; chiral HPLC ; (R) and (S) calmidazolium ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Calmidazolium {R24571, 1-[bis(4-chlorophenyl)methyl]-3-[2-(2,4-dichlorophenyl)-2-[(2,4-dichlorophenyl)methoxy]ethyl]-1H-imidazolium chloride} is a potent calmodulin inhibitor. This paper describes the synthesis and properties of the enantiomers of calmidazolium from the enantiomers of miconazole {1(N)-(2-(2,4-dichlorobenzyloxy)-2-(2,4-dichlorophenyl))-ethyl imidazole}, prepared from the racemate by chiral preparative scale high performance liquid chromatography. Overlap between ligand and protein resonances in the aromatic region of the 1H NMR spectrum of the calmidazolium-calmodulin complexes has been obviated by preparation of the protein with all of its nine phenylalanine rings deuterated (Phe-d5 calmodulin). This has been accomplished by the overexpression of calmodulin derived from Trypanosoma brucei rhodiesiense in E. coli in a medium supplemented with ring-deuterated phenylalanine. The kinetics of binding of each enantiomer are slow on the 1H NMR time scale as judged by the behaviour of the H2 resonance of Histidine-107, which is clearly visible under the sample conditions used. The aromatic spectral regions of the protein-bound (+) and (-) enantiomers contrast strikingly, reflecting differences in bound environment and/or conformation. Chirality 8:545-500, 1996. © 1997 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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