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  • 1
    Electronic Resource
    Electronic Resource
    Bovine β–lactoglobulin modified by 3–hydroxyphthalic anhydride blocks the CD4 cell receptor for HIV (1996)
    [s.l.] : Nature Publishing Group
    Nature medicine 2 (1996), S. 230-234 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Sexual transmission is the most frequent (86%) route of adult HIV–1 transmission worldwide1. In the absence of a prophylactic anti–HIV vaccine, other methods of preventing infection should be implemented. Virucidal spermicides have been considered for this purpose, but their ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nm0296-230
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Structural requirements for and consequences of an antiviral porphyrin binding to the V3 loop of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp120 (1995)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 8 (1995), S. 345-357 
    Details
    ISSN: 0952-3499
    Keywords: human immunodeficiency virus (HIV-1) ; envelope glycoprotein gp120 ; V3 loop ; porphyrin binding ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Several porphyrin derivatives were reported to have anti-HIV-1 activity. Among them, meso-teta(4-carboxyphenyl)porphine (MYCPP) and other carboxyphenyl derivatives were the most potent inhibitors (EC50 〈 0.7 μM). MTCPP bound to the HIV-1 enveloope glycoprotein gp120 and to full-length V3 loop peptides corresponding to several HIV-1 isolates but not to other peptides from gp120+gp41. However, it remained possible that MTCPP bound to HIV-1 envelop glycoprotein gp120 and to full-length V3 loop peptides corresponding to several HIV-1 isolates but not to other peptides from gp120+gp41. However, it remained possible that MTCPP bound to regions on gp120 which cannot be mimicked by peptides. Further characterization of the binding domain for MTCPP is important for understanding the antiviral activity of porphyrins and for the design of anit-HIV-1 drugs interfering with functions of the virus envelope. Results presented here show that: (i) deletion of the V3 loop from the gp120 sequence resulted in drastically diminished MTCPP binding, suggesting that the V3 loop is the dominant if not the only target site on gp120; (ii) this site was only partially mimicked by full-length V3 loop peptides; (iii) MTCPP binding to the gp120 V3 loop elicited allosteric effects resulting in decreased accessibility of the CD4 receptor binding site; (iv) the binding site for MTCPP lies within the central portion of the V3 loop (KSIHIGPGRAFY for the HIV-1 subtype B consensus sequence) and does not involve directly the GPG apex of the loop. These results may help in designing antiviral compounds with improved activity.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmr.300080604
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Blocking of CD4 cell receptors for the human immunodeficiency virus type 1 (HIV-1) by chemically modified bovine milk proteins: Potential for AIDS prophylaxis (1995)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 8 (1995), S. 304-316 
    Details
    ISSN: 0952-3499
    Keywords: human and simian immunodeficiency viruses ; CD4 cell receptor ; acid anhydrides ; monoclonal antibodies ; serum albumin ; casein ; milk ; prophylaxis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The chemical transformation of synthetic combinatorial libraries to increase the diversity of compounds of medicinal interest was reported recently. Chemical modification of natural products represents a complementary approach to accomplish this aim. Modification of lysines by aromatic acid anhydrides, preferentially by 3-hydroxyphthalic and trimellitic anhydrides and trimellitic anhydride chloride, converted commonly available proteins (human and bovine serum albumin and casein) into potent inhibitors of (i) binding between the HIV-1 gp120 envelope glycoprotein and the CD4 cell receptor, probably owing to their binding to CD4, and (ii) infection by HIV-1. Modified bovind milk proteins are also potent HIV-1 inhibitors and may have protential for anti-Hiv-1 prophylaxis.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmr.300080504
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    Paper (German National Licenses)
    Fulltext
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