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Incorporation of Putative Helix-Breaking Amino Acids in the Design of Novel Stapled Peptides: Explor...

Incorporation of Putative Helix-Breaking Amino Acids in the Design of Novel Stapled Peptides: Explor...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_76dd0b05d6584b64a066db0da685651e

Incorporation of Putative Helix-Breaking Amino Acids in the Design of Novel Stapled Peptides: Exploring Biophysical and Cellular Permeability Properties

About this item

Full title

Incorporation of Putative Helix-Breaking Amino Acids in the Design of Novel Stapled Peptides: Exploring Biophysical and Cellular Permeability Properties

Publisher

Switzerland: MDPI AG

Journal title

Molecules (Basel, Switzerland), 2019-06, Vol.24 (12), p.2292

Language

English

Formats

Publication information

Publisher

Switzerland: MDPI AG

More information

Scope and Contents

Contents

Stapled α-helical peptides represent an emerging superclass of macrocyclic molecules with drug-like properties, including high-affinity target binding, protease resistance, and membrane permeability. As a model system for probing the chemical space available for optimizing these properties, we focused on dual Mdm2/MdmX antagonist stapled peptides r...

Alternative Titles

Full title

Incorporation of Putative Helix-Breaking Amino Acids in the Design of Novel Stapled Peptides: Exploring Biophysical and Cellular Permeability Properties

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_76dd0b05d6584b64a066db0da685651e

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_76dd0b05d6584b64a066db0da685651e

Other Identifiers

ISSN

1420-3049

E-ISSN

1420-3049

DOI

10.3390/molecules24122292

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