A 'cross-stitched' peptide with improved helicity and proteolytic stability

Autor:	Sean W. Fanning, Zamia Siddiqui, Terry W. Moore, Emad Tajkhorshid, Geoffrey L. Greene, Christopher G. Mayne, Thomas E. Speltz
Rok vydání:	2018
Předmět:	Models Molecular Protein Conformation alpha-Helical 0301 basic medicine Stereochemistry Amino Acid Motifs Peptide 010402 general chemistry 01 natural sciences Biochemistry Article 03 medical and health sciences chemistry.chemical_compound Amino Acid Sequence Physical and Theoretical Chemistry chemistry.chemical_classification Binding Sites Bicyclic molecule Organic Chemistry Estrogen Receptor alpha Helicity 0104 chemical sciences 030104 developmental biology chemistry Proteolysis Lactam Peptides
Zdroj:	Organic & Biomolecular Chemistry. 16:3702-3706
ISSN:	1477-0539 1477-0520
Popis:	A new computational approach to obtain quantitative energy profiles for helix folding was used in the design of orthogonal hydrocarbon and lactam bicyclic peptides. The proteolytically stable, "cross-stitched" peptide SRC2-BCP1 shows nanomolar affinity for estrogen receptor α and X-ray crystallography confirms a helical binding pose.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a40f145e38726c53ba7e1af964c73eee https://doi.org/10.1039/c8ob00790j Zobrazit plný text záznamu