The solution structure of sarafotoxin-c. Implications for ligand recognition by endothelin receptors.

Mills, Robyn G.; Ralston, G.B.; King, Glenn F.

doi:10.1016/s0021-9258(17)31531-4

Cited by 14 publications

References 52 publications

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Oxidative folding of cystine‐rich peptides vs regioselective cysteine pairing strategies

et al. 1996

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The methodology of regioselective cysteine pairings in synthetic multiple‐cystine peptides has progressed in the past years to an efficiency that allows for at least three specific inter‐ and intrachain disulfide bridgings. Conformational studies on various multiple‐cystine peptides like hormones, protease inhibitors, and toxins revealed that these bioactive peptides, generated by posttranslational processing of precursor proteins, are folded into miniprotein‐like compact globular structures of remarkable stability. This strongly suggests protein domain or subdomain properties of these families of peptides, and thus sufficient sequence‐encoded information for correct oxidative refolding under appropriate experimental conditions. From intensive research on the mechanisms and pathways of oxidative refolding of proteins in vivo and in vitro, the efficient methods have emerged for simulating nature in the regeneration of native folds not only for intact proteins, but also for protein domains and subdomains. In fact, the results obtained in the oxidative folding of excised protein fragments and of relatively low mass products of posttranslational processings show that this procedure is indeed a simple way of preparing peptides with several disulfide bonds, if optimization of reaction conditions is performed in terms of redox buffer, temperature, and additives capable of disrupting aggregates and of stabilizing nascent secondary structures. Moreover, with increased knowledge about stable, small natural cystine frameworks, their use instead of artificial templates should facilitate engineering of synthetic miniproteins with specific conformation and tailored functions. © 1996 John Wiley & Sons, Inc.

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Oxidative folding of cystine‐rich peptides vs regioselective cysteine pairing strategies

et al. 1996

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Solution structure determination of endothelin-1 in methanol/water by NMR and molecular modelling methods

Hewage

Parkinson

et al. 1997

J. Peptide Sci.

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To understand the structural requirements for the biological activity of endothelin peptides and to develop receptor selective endothelin analogues further, the solution structure of the bicyclic 21 amino acid residue vasoactive peptide, endothelin-1, has been determined in methanol-d3/water using high-resolution 1H-NMR spectroscopy. To our knowledge, this solvent system has not previously been used in NMR studies of endothelin and/or endothelin-like peptides. Two-dimensional DQFCOSY, TOCSY and NOESY spectra were acquired along with a series of one-dimensional spectra. A total of 219 distance constraints and 5 angle constraints were derived from the NMR data. These were incorporated into structure calculations using distance geometry (DIANA) followed by simulated annealing and molecular dynamics. The resulting structures are characterized by an alpha-helical conformation, Lys9-His16, and residues Ser5-Asp8 form a type I beta-turn. The N-terminal region, which was not extensively constrained by NMR data, showed no preferred conformation. The C-terminal tail showed less extensive conformational averaging but no descriptive conformation could be observed. The results obtained in this study are in good agreement with previous proposals.

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Synthesis of single‐ and multiple‐stranded cystine‐rich peptides

et al. 2004

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The solution structure of sarafotoxin-c. Implications for ligand recognition by endothelin receptors.

Cited by 14 publications

References 52 publications

Oxidative folding of cystine‐rich peptides vs regioselective cysteine pairing strategies

Oxidative folding of cystine‐rich peptides vs regioselective cysteine pairing strategies

Solution structure determination of endothelin-1 in methanol/water by NMR and molecular modelling methods

Synthesis of single‐ and multiple‐stranded cystine‐rich peptides

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