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New peptide architectures through C–H activation stapling between tryptophan–phenylalanine/tyrosine...

New peptide architectures through C–H activation stapling between tryptophan–phenylalanine/tyrosine...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4455059

New peptide architectures through C–H activation stapling between tryptophan–phenylalanine/tyrosine residues

About this item

Full title

New peptide architectures through C–H activation stapling between tryptophan–phenylalanine/tyrosine residues

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2015-05, Vol.6 (1), p.7160-7160, Article 7160

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Natural peptides show high degrees of specificity in their biological action. However, their therapeutical profile is severely limited by their conformational freedom and metabolic instability. Stapled peptides constitute a solution to these problems and access to these structures lies on a limited number of reactions involving the use of non-natur...

Alternative Titles

Full title

New peptide architectures through C–H activation stapling between tryptophan–phenylalanine/tyrosine residues

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4455059

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4455059

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms8160

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