Titration and fluorometric studies of the tyrosine side chain of angiotensin II and related peptides

Juliano, Luiz; Laluce, Cecília; Oliveira, Maria C. F. de; Paiva, Antonio C. M.

doi:10.1002/bip.1979.360180716

Cited by 6 publications

(2 citation statements)

References 41 publications

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“…This contrasts with the spectral variations of 3-(NO2)-Tyr in this pH range, caused by dissociation of the hydroxyl group whose pK = 6.76 for the free amino acid, determined as previously described [25]. This contrasts with the spectral variations of 3-(NO2)-Tyr in this pH range, caused by dissociation of the hydroxyl group whose pK = 6.76 for the free amino acid, determined as previously described [25].…”

Section: Discussioncontrasting

confidence: 52%

Internally quenched fluorogenic protease substrates: Solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs

et al. 1995

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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~-Boc or -Fmoc derivative of glutamic acid with the a-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 a-amino group of proline showed that strong quenching of Abz fluorescence occurs in the absence of any acceptor group.

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Section: Discussioncontrasting

confidence: 52%

Internally quenched fluorogenic protease substrates: Solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs

et al. 1995

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“…arises from a change in the conformation of the A-II complex which occurs when the terminal amino group becomes protonated. This interpretation is supported by the fact that the terminal amine has a pKa of 7.6 in 2H2Q (Juliano et al, 1979) and by the observation that the angiotensin II peptides undergo a significant conformational change at this pH .…”

Section: Simon Unpublished Results)mentioning

confidence: 85%

Ionophoric properties of angiotensin II peptides. Nuclear magnetic resonance kinetic studies of the hormone-mediated transport of manganese ions across phosphatidylcholine bilayers

Degani¹,

Lenkinski²

1980

Biochemistry

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The linear peptide hormones angiotensin II and [Asn1, Val5]angiotensin II are found to mediate the transport of Mn(II) ions across phosphatidylcholine bilayers. Nuclear magnetic resonance spectroscopy (NMR) is applied to monitor the rate of transport of Mn(II) ions by measuring the rate of disappearance of the 1H NMR signal of the choline methyl groups of the inner phospholipid layer. This rate of disappearance is analyzed in terms of a pseudo-first-order rate equation for the transport process. The rate of transport of Mn(II) varies linearly with both the concentrations of Mn(II) and agiotensin II (A-II) present, suggesting that the ions are transported in a complex with 1:1 stoichiometry. An analysis of the temperature dependence of the rate of transport yielded an energy of activation of 29 +/- 5 kcal/mol and an entrophy of activation of 10 eu for the transport process. The activation parameters are discussed in terms of defining the rate-limiting step in the transport process. The pH dependence of the hormone-mediated rate of Mn(II) transport is similar to the pH dependence of the metal complexation process measured in a separate study. The presence of La(III) or Tris decelerates the rate of Mn(II) transport by presumably competing with either Mn(II) or A-II, respectively, in the binding process. On the basis of the results presented here as well as literature data, we suggest that the ionophoric properties of these two hormones may be relevant to understanding the role of metal ions in their physiological activities.

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The conformation of angiotensin II

Lenkinski¹,

Stephens²,

Krishna³

1981

Biochimica et Biophysica Acta (BBA) - Protein Structure

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Titration and fluorometric studies of the tyrosine side chain of angiotensin II and related peptides

Cited by 6 publications

References 41 publications

Internally quenched fluorogenic protease substrates: Solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs

Internally quenched fluorogenic protease substrates: Solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs

Ionophoric properties of angiotensin II peptides. Nuclear magnetic resonance kinetic studies of the hormone-mediated transport of manganese ions across phosphatidylcholine bilayers

The conformation of angiotensin II

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