Unequivocal assignments of NH proton magnetic resonance bands in oxytocin using <sup>2</sup>H‐ and <sup>15</sup>N‐substituted molecules

Bradbury, A. F.; Burgen, A. S. V.; Feeney, J.; Roberts, Gordon C. K.; Smyth, Derek G.

doi:10.1016/0014-5793(74)80780-5

Cited by 26 publications

(8 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The second analogue, desaminooxytocin (not shown), lacks the N-terminal amino group (Ferrier et al, 1965). Of these three peptides, only oxytocin has been extensively characterized in aqueous solution by NMR (Glickson et al, 1972;Richard-Brewster et al, 1973;Bradbury et al, 1974;Hruby, 1974;Glickson, 1975;Wyssbrod et al, 1977). In addition, the crystal structure of desaminooxytocin has been recently reported (Pitts et al, 1985).…”

mentioning

confidence: 99%

Time-resolved fluorescence and proton NMR studies of tyrosyl residues in oxytocin and small peptides: correlation of NMR-determined conformations of tyrosyl residues and fluorescence decay kinetics

et al. 1986

View full text Add to dashboard Cite

Steady-state and time-resolved fluorescence properties of the single tyrosyl residue in oxytocin and two oxytocin derivatives at pH 3 are presented. The decay kinetics of the tyrosyl residue are complex for each compound. By use of a linked-function analysis, the fluorescence kinetics can be explained by a ground-state rotamer model. The linked function assumes that the preexponential weighting factors (amplitudes) of the fluorescence decay constants have the same relative relationship as the 1H NMR determined phenol side-chain rotamer populations. According to this model, the static quenching of the oxytocin fluorescence can be attributed to an interaction between one specific rotamer population of the tyrosine ring and the internal disulfide bridge.

show abstract

mentioning

confidence: 99%

Time-resolved fluorescence and proton NMR studies of tyrosyl residues in oxytocin and small peptides: correlation of NMR-determined conformations of tyrosyl residues and fluorescence decay kinetics

et al. 1986

View full text Add to dashboard Cite

show abstract

“…Solid-Phase Synthesis of Boc-O-benzyltyrosylisoleucylglut-aminyIasparagmyl-S-3,4-dimethylbenzylcysteinylprolylleucylglycinate-Resin (22). Boc-leucylglycinate-resin with a substitution level of 0.36 mmol/g was prepared in an analogous manner to that described for the preparation of 19.…”

Section: Methodsmentioning

confidence: 99%

Synthesis of specifically deuterated S-benzylcysteines and of oxytocin and related diastereomers deuterated in the half-cystine positions

Upson¹,

Hruby²

1976

J. Org. Chem.

View full text Add to dashboard Cite

S-Benzylcysteine derivatives specifically deuterated at the a carbon only, the p carbon only, and at both the 01 and p carbons have been.synthesized. These labeled compounds have been enzymatically resolved and the enantiomers and reacemates have been converted to the N-tert-hutyloxycarbonyl derivatives. The deuterium labels were not exchanged under the conditions of the syntheses. Condensation of the sodium salt of difthyl a-acetamidomalonate with benzyl chloromethyl sulfide followed by hydrolysis with DCl afforded S-benzyl-DL-[a-*Hl]cysteine. Acetylation followed by treatment with hog renal acylase separated the stereoisomers. A Mannich reaction with [2H2]methylene diacetate, diethyl a-acetamidomalonate, and dimethylamine followed by quaternization of the amino nitrogen with methyl iodide gave diethyl a-acetamido-a-dimethylamino[2H~]methylmalonate methiodide (15). Treatment of 15 with sodium benzylmercaptide gave diethyl a-acetamid~-a-benzylthio[~H~]methylmalonate, which was hydrolyzed with HCl to yield S-ben~yl-DL-[P,/3-~Hz]cysteine or with DCl to afford S-benzyl-DL-[a,P,P-2H3]cysteine. These compounds were resolved as before. The preparation of S-benzyl-DL-[a,P,P-2H3] cysteine required an efficient source of ethanol-d. This deuterated solvent was prepared in quantitative yield in 2 h from tetraethoxysilane, D20, and a catalytic amount of thionyl chloride. The protected deuterated amino acids were used in the preparation of several oxytocin analogues in which the specific deuteration appears in either the 1-hemicystine or the 6-hemicystine residues.

show abstract

“…Such definite assignments can then be used in the interpretation of ' 3 C experiments which utilize the i3 C natural abundance spectra. l5 N enrichment of oxytocin has been used to define the assignment of NH protons in the proton nmr spectrum of the hormone [4]. Moreover, l3 C and ' 5 N enriched hormone molecules offer a new approach for characterizing conformational and microdynamical properties of neuro-168 hypophyseal peptides bound to their physiological carrier proteins, the neutophysins [5-81.…”

Section: Introductionmentioning

confidence: 99%

Carbon‐13 nuclear magnetic resonance studies on (85% ¹³C‐enriched Gly⁹) oxytocin

et al. 1975

View full text Add to dashboard Cite

Unequivocal assignments of NH proton magnetic resonance bands in oxytocin using ²H‐ and ¹⁵N‐substituted molecules

Cited by 26 publications

References 18 publications

Time-resolved fluorescence and proton NMR studies of tyrosyl residues in oxytocin and small peptides: correlation of NMR-determined conformations of tyrosyl residues and fluorescence decay kinetics

Time-resolved fluorescence and proton NMR studies of tyrosyl residues in oxytocin and small peptides: correlation of NMR-determined conformations of tyrosyl residues and fluorescence decay kinetics

Synthesis of specifically deuterated S-benzylcysteines and of oxytocin and related diastereomers deuterated in the half-cystine positions

Carbon‐13 nuclear magnetic resonance studies on (85% ¹³C‐enriched Gly⁹) oxytocin

Contact Info

Product

Resources

About

Unequivocal assignments of NH proton magnetic resonance bands in oxytocin using 2H‐ and 15N‐substituted molecules

Cited by 26 publications

References 18 publications

Time-resolved fluorescence and proton NMR studies of tyrosyl residues in oxytocin and small peptides: correlation of NMR-determined conformations of tyrosyl residues and fluorescence decay kinetics

Time-resolved fluorescence and proton NMR studies of tyrosyl residues in oxytocin and small peptides: correlation of NMR-determined conformations of tyrosyl residues and fluorescence decay kinetics

Synthesis of specifically deuterated S-benzylcysteines and of oxytocin and related diastereomers deuterated in the half-cystine positions

Carbon‐13 nuclear magnetic resonance studies on (85% 13C‐enriched Gly9) oxytocin

Contact Info

Product

Resources

About

Unequivocal assignments of NH proton magnetic resonance bands in oxytocin using ²H‐ and ¹⁵N‐substituted molecules

Carbon‐13 nuclear magnetic resonance studies on (85% ¹³C‐enriched Gly⁹) oxytocin