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  • 1
    Electronic Resource
    Electronic Resource
    Specificity of the Dynorphin-Processing Endoprotease: Comparison with Prohormone Convertases (1999)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 72 (1999), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The cleavage specificity of a monobasic processing dynorphin converting endoprotease is examined with a series of quench fluorescent peptide substrates and compared with the cleavage specificity of prohormone convertases. A dynorphin B-29-derived peptide, Abz-Arg-Arg-Gln-Phe-Lys-Val-Val-Thr-Arg-Ser-Glneddnp (where Abz is o-aminobenzoyl and eddnp is ethylenediamine 2,4-dinitrophenyl), that contains both dibasic and monobasic cleavage sites is efficiently cleaved by the dynorphin converting enzyme and not cleaved by two propeptide processing enzymes, furin and prohormone convertase 1. A shorter prorenin-related peptide, Dnp-Arg-Met-Ala-Arg-Leu-Thr-Leu-eddnp, that contains a monobasic cleavage site is cleaved by the dynorphin converting enzyme and prohormone convertase 1 and not by furin. Substitution of the P1’ position by Ala moderately affects cleavage by the dynorphin-processing enzyme and prohormone convertase 1. It is interesting that this substitution results in efficient cleavage by furin. The site of cleavage, as determined by matrix-assisted laser desorption/ionization time of flight mass spectrometry, is N-terminal to the Arg at the P1 position for the dynorphin converting enzyme and C-terminal to the Arg at the P1 position for furin and prohormone convertase 1. Peptides with additional basic residues at the P2 and at P4 positions also serve as substrates for the dynorphin converting enzyme. This enzyme cleaves shorter peptide substrates with significantly lower efficiency as compared with the longer peptide substrates, suggesting that the dynorphin converting enzyme prefers longer peptides that contain monobasic processing sites as substrates. Taken together, these results suggest that the cleavage specificity of the dynorphin converting enzyme is distinct but related to the cleavage specificity of the prohormone convertases and that multiple enzymes could be involved in the processing of peptide hormones and neuropeptides at monobasic and dibasic sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1999.0722120.x
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  • 2
    Electronic Resource
    Electronic Resource
    Conformations of synthetic tetradecapeptide renin substrate and of angiotensin I in aqueous solution (1977)
    s.l. : American Chemical Society
    Biochemistry 16 (1977), S. 2606-2611 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00631a005
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  • 3
    Electronic Resource
    Electronic Resource
    Ionization of methyl derivatives of imidazole, histidine, thyreotropin releasing factor, and related compounds (1976)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 98 (1976), S. 7645-7648 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja00440a033
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  • 4
    Electronic Resource
    Electronic Resource
    Conserved cystatin segments as models for designing specific substrates and inhibitors of cysteine proteinases (1995)
    Springer
    The protein journal 14 (1995), S. 645-653 
    Details
    ISSN: 1573-4943
    Keywords: Cysteine proteinase ; cystatin ; diazomethylketone ; peptidyl fluorogenic substrate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Peptide segments derived from consensus sequences of the inhibitory site of cystatins, the natural inhibitors of cysteine proteinases, were used to develop new substrates and inhibitors of papain and rat liver cathepsins B, H, and L. Papain hydrolyzedAbz-QVVAGA-EDDnp andAbz-LVGGA-EDDnp at about the same rate, with specificity constants in the 107M−1 sec−1 range; cathepsin L also hydrolyzes both substrates with specificity constants in the 105 M−1 sec−1 range due to lowerk cat values, with theK m 's being identical to those with papain. OnlyAbz-LVGGA-EDDnp was rapidly hydrolyzed by cathepsin B, and to a lesser extent by cathepsin H. Peptide substrates that alternate these two building blocks (LVGGQVVAGAPWK and QVVAGALVGGAPWK) discriminate the activities of cathepsins B and L and papain. Cathepsin L was highly selective for cleavage at the G-G bond of the LVGG fragment in both peptides. Papain and cathepsin B cleaved either the LVGG fragment or the QVVAG fragment, depending on their position within the peptide. While papain was more specific for the segment located C-terminally, cathepsin B was specific for that in N-terminal position. Peptidyl diazomethylketone inhibitors based on these two sequences also reacted differently with papain and cathepsins. GlcA-QVVA-CHN2 was a potent inhibitor of papain and reacted with papain 60 times more rapidly (k +0= 1,100,000 M−1 sec−1) than with cathepsin L, and 220 times more rapidly than with cathepsin B. Cathepsins B and L were preferentially inhibited by Z-RLVG-CHN2. Thus cystatin-derived peptides provide a valuable framework for designing sensitive, selective substrates and inhibitors of cysteine proteinases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01886903
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  • 5
    Electronic Resource
    Electronic Resource
    Titration and fluorometric studies of the tyrosine side chain of angiotensin II and related peptides (1979)
    New York : Wiley-Blackwell
    Biopolymers 18 (1979), S. 1793-1807 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The effect of charged side chains on the ionization and fluorescence of the Tyr4 phenolic group in angiotensin (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe) was investigated. Several synthetic peptides related to angiotensin were titrated spectrophotometrically and quantum yields of tyrosine fluorescence were also determined. The electrostatic interactions were interpreted according to the Kirkwood-Tanford theory, and the results were related to a recently proposed model [J. L. De Coen and E. Ralston (1977) Biopolymers 16, 1929] for angiotensin conformation in solution. The titration and fluorescence results are in good agreement with the folded conformations of this model, with the exception that the data indicate a weaker interaction between the histidine side chain and the C-terminal carboxyl groups than that proposed in the model.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1979.360180716
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  • 6
    Electronic Resource
    Electronic Resource
    Reduction of ortho-aminobenzoyl-proline fluorescence and formation of pyrrolobenzodiazepine-5,11-dione (1998)
    Springer
    International journal of peptide research and therapeutics 5 (1998), S. 19-28 
    Details
    ISSN: 1573-3904
    Keywords: ortho-aminobenzoyl-proline ; peptide synthesis ; protease fluorescent substrate ; pyrrolobenzodiazepine-5,11-dione
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The ortho-aminobenzoic acid (Abz) group is widely employed as a fluorescent marker for peptides used as substrates for the study of proteolytic enzyme activity. In fact, a direct correlation has been observed between fluorescence intensity and enzyme activity. An unusual behavior of the fluorescence properties of this group, which would lead to erroneous evaluation of the enzyme activity, was observed when it is bound directly to proline. Here we report a systematic NMR, fluorescence and X-ray diffraction study of the compounds obtained from Boc-Abz-Pro-NH2, Boc-Abz-Pro-OH, as well as from various other Boc-Abz-Pro-X derivatives, after treatment with HCl or TFA under anhydrous conditions. We verified that, as recently reported, even under these synthetic conditions, deprotection of Boc-Abz-Pro-NH2 or Boc-Abz-Pro-OH leads to the formation of the same product: pyrrolobenzodiazepine-5,11-dione. However, the formation of this compound was not detected with Abz-Pro-N(CH3)2, Abz-Pro-Leu-Gly-NH2 or Abz-pyrrolidine. For all these compounds we observed an unusual behavior for the fluorescence quantum yield of Abz that can be explained as the consequence of a non-radiative deactivation process produced, specifically, by the amidation of the Abz carboxyl group with proline or a similar secondary amine such as pyrrolidine. In conclusion, these results indicate that Abz cannot be used as an internal fluorescence marker for proteolytic enzyme activity when bound directly to proline.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008854301504
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  • 7
    Electronic Resource
    Electronic Resource
    Reduction ofortho-aminobenzoyl-proline fluorescence and formation of pyrrolobenzodiazepine-5,11-dione (1998)
    Springer
    International journal of peptide research and therapeutics 5 (1998), S. 19-28 
    Details
    ISSN: 1573-3904
    Keywords: ortho-aminobenzoyl-proline ; peptide synthesis ; protease fluorescent substrate ; pyrrolobenzodiazepine-5,11-dione
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Theortho-aminobenzoic acid (Abz) group is widely employed as a fluorescent marker for peptides used as substrates for the study of proteolytic enzyme activity. In fact, a direct correlation has been observed between fluorescence intensity and enzyme activity. An unusual behavior of the fluorescence properties of this group, which would lead to erroneous evaluation of the enzyme activity, was observed when it is bound directly to proline. Here we report a systematic NMR, fluorescence and X-ray diffraction study of the compounds obtained from Boc-Abz-Pro-NH2, Boc-Abz-Pro-OH, as well as from various other Boc-Abz-Pro-X derivatives, after treatment with HCl or TFA under anhydrous conditions. We verified that, as recently reported, even under these synthetic conditions, deprotection of Boc-Abz-Pro-NH2 or Boc-Abz-Pro-OH leads to the formation of the same product: pyrrolobenzodiazepine-5,11-dione. However, the formation of this compound was not detected with Abz-Pro-N(CH3)2, Abz-Pro-Leu-Gly-NH2 or Abz-pyrrolidine. For all these compounds we observed an unusual behavior for the fluorescence quantum yield of Abz that can be explained as the consequence of a non-radiative deactivation process produced, specifically, by the amidation of the Abz carboxyl group with proline or a similar secondary amine such as pyrrolidine. In conclusion, these results indicate that Abz cannot be used as an internal fluorescence marker for proteolytic enzyme activity when bound directly to proline.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443536
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  • 8
    Electronic Resource
    Electronic Resource
    Internally quenched fluorogenic protease substrates: Solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs (1995)
    Springer
    International journal of peptide research and therapeutics 1 (1995), S. 299-308 
    Details
    ISSN: 1573-3904
    Keywords: Protease fluorescent substrate ; Renin ; Tissue kallikrein ; Peptide synthesis ; Ortho-aminobenzoyl-proline
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary A general procedure, using the commonly employed solid-phase peptide synthesis methodology for obtaining internally quenched fluorogenic peptides with ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs, is presented. The essential feature of this procedure is the synthesis of an N α-Boc or-Fmoc derivative of glutamic acid with the α-carboxyl group bound to N-(2,4-dinitrophenyl)-ethylenediamine (EDDnp), which provides the quencher moiety attached to the C-terminus of the substrate. The fluorescent donor group, ortho-aminobenzoic acid (Abz), is incorporated into the resin-bound peptide in the last coupling cycle. Depending on the resin type used, Abz-peptidyl-Gln-EDDnp or Abz-peptidyl-Glu-EDDnp is obtained. Using the procedure described above, substrates for human renin and tissue kallikreins were synthesised. Spectrofluorimetric measurements of Abz bound to the α-amino group of proline showed that strong quenching of Abz fluorescence occurs in the absence of any acceptor group.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00119771
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  • 9
    Electronic Resource
    Electronic Resource
    Fluorescent properties of amino acids labeled with ortho-aminobenzoic acid (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 395-402 
    Details
    ISSN: 1075-4261
    Keywords: ortho-aminobenzoylamino acids ; fluorescence ; protease ; peptide ; peptide synthesis ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: ortho-Aminobenzoic acid (Abz) has been used as a convenient fluorescent donor group in internally quenched fluorescent peptides, which are employed as substrates for several proteolytic enzymes. As Abz is usually bound to the N-amino terminal of these peptides, it is of interest to investigate the Abz group fluorescent properties bound to different amino acids. We report in this article the optical absorption and fluorescent properties, in aqueous media, of Abz bound to the α-amino group of Ala, Gly, Leu, Ile, Val, Pro, Phe, Arg, Glu, Met, Asn, Tyr, and Trp, with monomethyl-amidated α-carboxyl group. In order to explore the origin of the drastic reduction of Abz attached to Nα amino group of prolyl-peptides, we also examined the fluorescence properties of Abz-NHCH3, Abz-N(CH3)2, and Abz-pyrrolidine. Molecular dynamics simulation and NMR data indicated a lack of periplanarity of the Abz-dimethylamide, which could be the origin of low fluorescence quantum yield of Abz-prolyl-peptides. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 395-402, 1998
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Inhibition of cruzipain visualized in a fluorescence quenched solid-phase inhibitor library assay. D-Amino Acid Inhibitors for cruzipain, cathepsin B and cathepsin L (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 4 (1998), S. 83-91 
    Details
    ISSN: 1075-2617
    Keywords: fluorescence quenched assay ; inhibitor library ; Trypanosoma cruzi ; cathepsin B and L inhibitors ; Parasitic protease inhibition ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A PEGA-resin was derivatized with a 3:1 mixture of hydroxymethyl benzoic acid and Fmoc-Lys(Boc)-OH and the fluorogenic substrate Ac-Y(NO2)KLRFSKQK(Abz)-PEGA was assembled on the lysine using the active ester approach. Following esterification of the hydroxymethyl benzoic acid with Fmoc-Val-OH a library XXX-k/r-XXXV containing approximately 200,000 beads was assembled by split synthesis. The resulting ‘one bead, two peptides’ library was subjected to extensive hydrolysis with cruzipain. One hundred darker beads were isolated and the 14 most persistently dark beads were collected and sequenced. The putative inhibitor peptides and several analogues were synthesized and found to be competitive μM to nM inhibitors of cruzipain in solution. The inhibitory activity was found to be unspecific to cruzipain when compared with cathepsins B and L and specific when compared with kallikrein. One of the inhibitors was docked into the active site of the cathepsin B and was found most probably to bind to the enzyme cavity in an unusual manner, owing to the inserted D-amino acid residue. © 1998 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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