Opioid peptides in micellar systems: Conformational analysis by CD and by one‐dimensional and two‐dimensional <sup>1</sup>H‐nmr spectroscopy

Zetta, Lucia; Consonni, Roberto; Marco, A. De; Longhi, Renato; Manera, Ernesto; Vecchio, Giuseppe

doi:10.1002/bip.360300905

Cited by 15 publications

(8 citation statements)

References 33 publications

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“…Alternatively, the need to vary the receiver gain could be overcome by employing pulse-gradient techniques to suppress the water signal. Indeed, when the WATERGATE sequence (Piotto et al, 1992) was employed to achieve water suppression, the cross-peak volumes measured in the presence of the paramagnetic probe never exceeded the micelles (Zetta and Kaptein, 1984; Zetta et al, 1990) In the presence of TEMPOL, the cross-peaks relative to K15 and A25 disappeared. The single-letter amino acid code is used for labeling the cross-peak assignments.…”

Section: Resultsmentioning

confidence: 99%

Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor

Molinari

Esposito

Ragona

et al. 1997

Biophysical Journal

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In the absence of specific interactions, the relative attenuation of protein NMR signals due to added stable free radicals such as TEMPOL should reflect the solvent accessibility of the molecular surface. The quantitative correlation between observed attenuation and surface accessibility was investigated with a model system, i.e., the small protein bovine pancreatic trypsin inhibitor. A detailed discussion is presented on the reliability and limits of the approach, and guidelines are provided for data acquisition, treatment, and interpretation. The NMR-derived accessibilities are compared with those obtained from x-ray diffraction and molecular dynamics data. Although the time-averaged accessibilities from molecular dynamics are ideally suited to fit the NMR data, better agreement was observed between the paramagnetic attenuations of the fingerprint cross-peaks of homonuclear proton spectra and the total NH and H alpha accessibilities calculated from x-ray coordinates, than from time-averaged molecular dynamics simulations. In addition, the solvent perturbation response appears to be a promising approach for detecting the thermal conformational evolution of secondary structure elements in proteins.

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Section: Resultsmentioning

confidence: 99%

Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor

Molinari

Esposito

Ragona

et al. 1997

Biophysical Journal

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“…Opioid peptides have often been studied in media similar to the membrane environment, usually aqueous micellar solutions. The micelles generally used are based on SDS, a detergent easy to find in perdeuterated form [26][27][28][29], but there are also published studies of micelles of phospholipids [30][31][32][33][34][35][36].…”

Section: Membranesmentioning

confidence: 99%

Solution structure of nociceptin peptides

Amodeo

Guerrini

Picone

et al. 2002

Journal of Peptide Science

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Peptides embedded in the sequence of pre-pro-nociceptin, i.e. nociceptin, nocistatin and orphanin FQ2, have shed light on the complexity of the mechanisms involving the peptide hormones related to pain and have opened up new perspectives for the clinical treatment of pain. The design of new ligands with high selectivity and bioavailability, in particular for ORL1, is important both for the elucidation and control of the physiological role of the receptor and for their therapeutic importance. The failure to obtain agonists and antagonists when using, for nociceptin, the same substitutions that are successful for opioids, and the conformational flexibility of them all, justify systematic efforts to study the solution conformation under conditions as close as possible to their natural environment. Structural studies of linear peptides in solution are hampered by their high flexibility. A direct structural study of the complex between a peptide and its receptor would overcome this difficulty, but such a study is not easy since opioid receptors are membrane proteins. Thus, conformational studies of lead peptides in solution are still important for drug design. This review deals with conformational studies of natural pre-nociceptin peptides in several solvents that mimic in part the different environments in which the peptides exert their action. None of the structural investigations yielded a completely reliable bioactive conformation, but the global conformation of the peptides in biomimetic environments can shed light on their interaction with receptors.

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“…The role of the lipid phase of the membrane to facilitate ligand-receptor interactions has been addressed earlier for many biologically active peptides such as melittin, glucagon and enkephalins (32)(33)(34)(35)(36)(37)(38)(39)(40). SP is stored in vesicles at the terminals of presynaptic neurons and binds specifically to a protein receptor embedded in the postsynaptic membrane.…”

Section: Introductionmentioning

confidence: 99%

Lipid-induced Conformation of Substance P

Cowsik

Lücke

Rüterjans

1997

Journal of Biomolecular Structure and Dynamics

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Both the aqueous and the lipid-induced structure of a representative and widely studied tachykinin, substance P, has been investigated by two-dimensional proton nuclear magnetic resonance (2D 1H-NMR) spectroscopy and distance geometry calculations. Unambiguous NMR assignments of protons have been made with the aid of correlation spectroscopy (COSY and TOCSY) experiments and Overhauser enhancement spectroscopy (ROESY and NOESY; experiments. The NMR data obtained were utilized in a distance geometry algorithm to generate a family of structures which were further refined using restrained energy minimization. These data show that, while in water substance P appears to favour an extended chain conformation, in the presence of perdeuterated dodecylphosphocholine (DPC) micelles as membrane model system an amphiphilic helical conformation is induced in the mid-region (Q5-Q8) of substance P. The conformation adopted by substance P in the presence of DPC micelles yields a structural motif typical of neurokinin-1 selective ligands, as proposed by Convert and coworkers (O. Convert et al., Neuropeptides 19, 259-270 (1991)).

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Opioid peptides in micellar systems: Conformational analysis by CD and by one‐dimensional and two‐dimensional ¹H‐nmr spectroscopy

Cited by 15 publications

References 33 publications

Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor

Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor

Solution structure of nociceptin peptides

Lipid-induced Conformation of Substance P

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Opioid peptides in micellar systems: Conformational analysis by CD and by one‐dimensional and two‐dimensional 1H‐nmr spectroscopy

Cited by 15 publications

References 33 publications

Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor

Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor

Solution structure of nociceptin peptides

Lipid-induced Conformation of Substance P

Contact Info

Product

Resources

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Opioid peptides in micellar systems: Conformational analysis by CD and by one‐dimensional and two‐dimensional ¹H‐nmr spectroscopy