A highly efficient route to dehydroalanine containing peptides

Burrage, Sarah; Raynham, Tony; Bradley, Mark

doi:10.1016/s0040-4039(98)00258-5

Cited by 20 publications

(11 citation statements)

References 12 publications

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“…Peptide 3 (see Figure 4) containing two dehydroamino acids and one cysteine residue was prepared by a novel method, developed for the incorporation of multiple dehydroamino acids into peptides. [25] This was achieved by the synthesis of peptides containing S-methylcysteine and the pyrolytic elimination of the S-methylcysteine sulfoxides. [25] The use of S-methylcysteine obviated the need for side chain protection, and if desired, Fmoc/tBu orthogonality could be maintained throughout the synthesis.…”

Section: Resultsmentioning

confidence: 99%

“…[25] This was achieved by the synthesis of peptides containing S-methylcysteine and the pyrolytic elimination of the S-methylcysteine sulfoxides. [25] The use of S-methylcysteine obviated the need for side chain protection, and if desired, Fmoc/tBu orthogonality could be maintained throughout the synthesis. It was envisaged that oxidation and elimination would be performed immediately prior to global deprotection.…”

Section: Resultsmentioning

confidence: 99%

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Biomimetic Synthesis of Lantibiotics

et al. 2000

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The lantibiotics are a class of highly posttranslationally modified small peptide antibiotics containing numerous lanthionine and dehydroamino acid residues. We have prepared peptides containing multiple dehydroamino acids and cysteine residues in order to probe the biomimetic synthesis of the lantibiotics from their precursor peptides. A novel synthetic methodology was developed to allow the synthesis of multiple dehydroamino acid containing peptides. Cyclisations were rapid, quantitative and regiospecific. Remarkably the peptide sequences alone appear to contain sufficient information to direct a series of stereo- and regiospecific ring closures. Thus both the two linear peptides for the B and E-rings closed stereoselectively. In the case of the A-ring precursor peptide which contained two dehydroamino acids, cyclisation was again totally regioselective, although not totally stereoselective.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Biomimetic Synthesis of Lantibiotics

et al. 2000

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“…Bradley and co-workers have introduced a dehydroalanine residue into peptides from commercially available S-methyl cysteine [10]. In this respect, peptides containing S-methyl cysteine was oxidatively eliminated to yield the desired dehydroamino acid derivatives (Scheme 6 ).…”

Section: Modification Of Peptides By Formationmentioning

confidence: 99%

Post-assembly Peptide Modifications by Chemical Methods

Kotha¹,

Lahiri

2005

CMC

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The demand for peptide drugs is increasing and in this context, "post-assembly (or post-translational) peptide modification strategies" by chemical manipulation of intact oligo-peptides has provided several analogues. Compounds prepared by this method are useful therapeutic molecules for structure activity studies. Herein, we describe various chemical methods such as cross-coupling reactions, cycloaddition reactions, radical reactions and ring-closing metathesis reactions that are useful for post-translational peptide modifications.

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“…[62] The drawback of this methodology lies in its reported incompatibility with protected Cys residues. [63] An alternative facile, site-specific and chemoselective method for introducing dehydroalanine into globally deprotected peptides employs Se-phenylselenocysteine. This amino acid can be conveniently incorporated into peptides by using standard SPPS (see Section 2.2.…”

Section: Synthesis Of Dehydropeptides and Their Use For Chemoselectivmentioning

confidence: 99%