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  • Aprotinin  (2)
  • Basic pancreatic trypsin inhibitor  (1)
  • HIV infection  (1)
  • 1
    Electronic Resource
    Electronic Resource
    1H NMR studies at 360 Mhz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI) (1977)
    Springer
    European biophysics journal 3 (1977), S. 303-315 
    Details
    ISSN: 1432-1017
    Keywords: NMR ; Proteinase inhibitor ; Protein modification ; Protein structure ; Basic pancreatic trypsin inhibitor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract In the 1H NMR spectra obtained at 360 MHz after digital resolution enhancement, the multiplet resonances of the methyl groups in the basic pancreatic trypsin inhibitor (BPTI) were resolved. With suitable double irradiation techniques the individual methyl resonances were assigned to the different types of aliphatic amino acid residues. Furthermore, from pH titration and comparison of the native protein with chemically modified BPTI, the resonance lines of Ala 16 in the active site and Ala 58 at the C-terminus were identified. Potential applications of the resolved methyl resonances as natural NMR probes for studies of the molecular conformations are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00535703
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Enzymatic semisynthesis of aprotinin homologues mutated in P′ positions (1991)
    Springer
    The protein journal 10 (1991), S. 245-251 
    Details
    ISSN: 1573-4943
    Keywords: Aprotinin ; bovine pancreatic trypsin inhibitor ; enzymatic synthesis ; semisynthesis ; inhibitory specificity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The replacement of amino acids in the P′1 and P′2 position of aprotinin, the bovine pancreatic trypsin inhibitor, is described. Using the “modified” inhibitor as starting material, with the hydrolyzed reactive-site peptide bond Lys15-Ala16, the residues P′1 (Ala16) and P′2 (Arg17) were split off by the action of aminopeptidase K. Incorporation of suitable dipeptides containing a basic residue (Lys or Arg) in the C-terminal position was carried out in a “one pot” reaction involving trypsin-catalyzed coupling. In this way, the native fragment Ala16-Arg17 was reintroduced and also replaced by Gly-Arg, Ala-Lys, and Leu-Arg yielding intact inhibitor molecules. The mechanism for incorporation of dipeptides was investigated by treating the aprotinin derivative with the Arg17-Ile18 peptide bond hydrolyzed with trypsin under proteosynthetic conditions. We established that only inhibitor molecules cleaved between Lys15 and Xaa16 are intermediates leading to the desired products. The inhibitory properties of the new aprotinin homologues were tested, and the significance of the P′1 residue for the inhibition of trypsin, kallikrein, and chymotrypsin was deduced.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024788
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  • 3
    Electronic Resource
    Electronic Resource
    Chemical semisynthesis of aprotinin homologues and derivatives mutated inp′ positions (1991)
    Springer
    The protein journal 10 (1991), S. 527-533 
    Details
    ISSN: 1573-4943
    Keywords: Aprotinin ; bovine pancreatic trypsin inhibitor ; semisynthesis ; inhibitory specificity ; kallikrein inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract An extended concept for the replacement of amino acids in theP' region of aprotinin by chemical semisynthesis is presented. Either fragment condensation with dipeptides protected as tert-butyl ester or stepwise introduction of two single amino acid-tert-butyl esters into a partially esterified aprotinin derivative (with free Lys15-carboxyl group) lacking the amino acids Ala16 and Arg17 leads to aprotinin homologues and derivatives mutated in theP′ 1 andP′ 2 position. This method may complement the recently reported enzymatic synthesis by enabling access to aprotinin homologues and derivatives, which cannot be prepared enzymatically. The synthesis of [Ala17]BPTI and [seco-17/18]BPTI is described in detail.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025481
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  • 4
    Electronic Resource
    Electronic Resource
    Inhibition of Tryptase TL2 from Human T4+ Lymphocytes and Inhibition of HIV-1 Replication in H9 Cells by Recombinant Aprotinin and Bikunin Homologues (1997)
    Springer
    The protein journal 16 (1997), S. 651-660 
    Details
    ISSN: 1573-4943
    Keywords: Kunitz-type inhibitor ; aprotinin ; bikunin ; tryptase TL2 ; HIV infection
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The serine esterase TL2 from human T4+ lymphocytes is a binding component to HIV-1 glycoprotein gp120 and seems to play a role in the HIV-1 infection mechanism. Recombinant variants of the Kunitz-type serine proteinase inhibitor aprotinin were investigated for their ability to inhibit tryptase TL2 and the binding of gp120 to this enzyme. Furthermore, the viral replication of HIV-1 was investigated in H9 cell cultures under the influence of recombinant aprotinin and bikunin variants. In contrast to native aprotinin, the recombinant variant [Arg15, Phe17, Glu52]aprotinin with a reactive-site sequence homologous to the V3 loop of HIV-1 gp120 showed a specific inhibition of tryptase TL2 (〉80%). However, the [Leu15, Phe17, Glu52]aprotinin variant with hydrophobic subsites was the most potent inhibitor of the binding of gp120 to tryptase TL2 (68%). Our results show that the enzyme activity of purified tryptase TL2 is inhibited not only by variants with basic amino acids, but also those with hydrophobic residues in the reactive-site region. Therefore, tryptase TL2 is not a typical trypsin-like or chymotrypsin-like protease. Investigations on inhibition of HIV-1 replication in H9 cell cultures showed that tryptase TL2 is involved in the mechanism of virus internalization into human lymphocytes. The [Leu15, Phe17, Glu52]aprotinin showed a significant retardation of syncytium formation over a period of 5 days in a 1 μM concentration. Similar investigations were performed with recombinant variants of bikunin, the light chain of human inter-α-trypsin inhibitor. Only the single-headed variant [Arg94]82bikunin inhibited slightly the syncytium formation over a period of 2 days in a 2.2 μM concentration. Wild-type bikunin and all full-length variants showed no effect, possibly due to steric hindrance by the second domain of the double-headed inhibitor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026379109403
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    Paper (German National Licenses)
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