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Inside Cover: Stapled Peptides with γ‐Methylated Hydrocarbon Chains for the Estrogen Receptor/Coactivator Interaction (Angew. Chem. Int. Ed. 13/2016)
Author(s) -
Speltz Thomas E.,
Fanning Sean W.,
Mayne Christopher G.,
Fowler Colin,
Tajkhorshid Emad,
Greene Geoffrey L.,
Moore Terry W.
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201601641
Subject(s) - chemistry , isoleucine , side chain , estrogen receptor , coactivator , stereochemistry , leucine , amino acid , cover (algebra) , molecular dynamics , biochemistry , organic chemistry , biology , computational chemistry , polymer , mechanical engineering , cancer , breast cancer , gene , transcription factor , engineering , genetics
Mimicking protein side chains with a functionalized hydrocarbon “staple” can affect the conformation and/or affinity for a protein target. In their Communication on page 4252 ff., T. W. Moore and co‐workers address the structural implications of replacing leucine and isoleucine residues with γ‐methyl‐substituted stapling amino acids. X‐ray crystal structures and molecular dynamics simulations provide a molecular understanding of the conformations of stapled peptides bound to estrogen receptor α.