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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 278 (1973), S. 301-312 
    ISSN: 1432-1912
    Keywords: Circular Dichroism ; Benzodiazepines ; Albumin-Binding ; Partition Coefficients
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The circular dichroism spectra of 12 benzodiazepine derivatives studied in presence of human serum albumin are presented. Nearly all substances give biphasic extrinsic Cotton effects. At the CD maxima the molar ellipticities and the anisotropy factors are calculated. The influence of the chemical structure of the benzodiazepines on the induced Cotton effect is discussed. There is a linear correlation between the anisotropy factors and the logarithms of the partition coefficients of the substances. It is suggested that the phenyl ring of the benzodiazepine molecule is one of the essential groups for the binding of these substances to human serum albumin.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 280 (1973), S. 229-237 
    ISSN: 1432-1912
    Keywords: Benzodiazepines ; Albumin Binding ; Gel Filtration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The binding of eleven benzodiazepine derivatives to human serum albumin (HSA) was determined by means of sephadex gel filtration. The albumin binding of the substances was characterized by the percentage of bound drug, the binding constants k +, K 1 and m, the number of binding sites per albumin molecule, and the free binding energy. Under the conditions chosen in these experiments there seems to exist only one binding site of the same type for all investigated benzodiazepines at the HSA molecule. The affinities of the benzodiazepines to this binding site are very different. It is discussed which part of the benzodiazepine molecule represents the main binding group.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 283 (1974), S. 67-82 
    ISSN: 1432-1912
    Keywords: Benzodiazepines ; Albumin Binding ; Circular Dichroism ; Gel Filtration ; pH Dependence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The influence of pH on the binding of benzodiazepine derivatives to HSA was studied by circular dichroism measurements and by gel filtration. The binding of nearly all benzodiazepines is increased by rising the pH from 6.60 to 8.20. For flurazepam, clonazepam, and nitrazepam this increase in binding is due to an increase of the affinities, while for the other substances the affinity remains constant and the number of binding sites is increased from one to two. The changes in binding of the benzodiazepines by rising the pH are explained by a cationic amino acid residue near or at the benzodiazepine binding site of the HSA molecule. This second binding site is not detectable by circular dichroism. For several of the substances rising the pH from 6.60 to 8.20, is accompanied by large alterations of the optical properties of the HSA-benzodiazepine complexes. These alterations are explained by changes of the asymmetric environment of the benzodiazepine binding site at the HSA molecule in the structural transition at slightly alkaline pH values. To explain the different reactions of the benzodiazepines within the N→B transition a theory is given.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 288 (1975), S. 17-27 
    ISSN: 1432-1912
    Keywords: Human Serum Albumin Binding ; l-Tryptophan ; Displacing Agents ; Benzodiazepines
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary By means of the gel filtration technique, the effect of nine benzo-diazepine derivates on the binding of l-tryptophan to human serum albumin was investigated. Using equimolar tryptophan and benzodiazepine concentrations, all benzodiazepines with binding constants higher than 104 (M−1), displace l-tryptophan from its binding site to a high degree. The mechanism of the displacement was characterized as a competition for a common binding site. Some of the benzodiazepines displace l-tryptophan to a greater extent than salicylic acid. The benzodiazepines and tryptophan are the only substances known with a high degree of stereospecific binding to human serum albumin. This study shows that there is only one binding site on the human serum albumin molecule, which binds tryptophan and the benzodiazepines in a highly stereospecific manner. Therefore it is concluded that the benzodiazepines and l-tryptophan must have similarities in their molecular structure, so that both can bind to the common binding site in such specific manner. These considerations are discussed in regard to the known influence of benzodiazepine derivatives on the l-tryptophan metabolism in brain. A direct involvement of the reported displacement in the pharmacological actions of the drugs seems not to be relevant because of their small therapeutical plasma levels.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 17 (1971), S. 1499-1501 
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Stamford, Conn. [u.a.] : Wiley-Blackwell
    Polymer Engineering and Science 29 (1989), S. 954-959 
    ISSN: 0032-3888
    Keywords: Chemistry ; Chemical Engineering
    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: In this paper we describe the synthesis, characterization, and lithographic evaluations of novel positive photoresists based on hydroxy polyimides and polyamides containing 6-F linking groups. The polymers were synthesized using solution condensation techniques and characterized using solution viscosity, GPC, FTIR, NMR, UV, TGA, and DSC. Tg's of these polymers range from 250 to 300°C. Both polyimides and polyamides are soluble in a variety of solvents commonly utilized for photoresist applications. When formulated with diazonaphthoquinone sensitizers, these polymers provide an improved high-temperature resistant, aqueous base developable positive photoresist system with good photospeed, contrast, and resolution characteristics. High resolution relief images were obtained which are comparable to 1300 Series AZ type photoresists. No thermal deformation, loss in resolution or defects were noticed when relief patterns were annealed to 250°C. Additionally, the hydroxy polyamide based resists, when thermally annealed to 300°C, provide a photoresist system with even higher thermal stability (400 to 450°C) and excellent resistance to solvents. Also, the photoresist formulations have excellent storage stability at room temperature and can be processed like conventional positive photoresists using broad band UV radiation sources.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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