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Publication year - 2019
Publication title -
peptide science
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.533
H-Index - 7
ISSN - 2475-8817
DOI - 10.1002/pep2.24115
Subject(s) - cover (algebra) , computer science , chirality (physics) , image (mathematics) , peptide , chemistry , combinatorics , stereochemistry , information retrieval , crystallography , physics , mathematics , artificial intelligence , biochemistry , engineering , mechanical engineering , chiral symmetry breaking , quantum mechanics , nambu–jona lasinio model , quark
Side chain cross‐linking is a commonly used strategy to stabilize peptides into a fixed secondary structure. Shi et al . describe all‐hydrocarbon tethered chirality induced helical peptides, reporting that the absolute configuration of a precisely positioned chiral center on the cross‐link dominates the peptides' secondary structure. The ensuing biophysical properties, including helical content, serum stability, cellular uptake and binding affinity with MDM2, differ from the thioether‐tethered counterparts. The approach provides a platform to evaluate the functional differences of peptides caused solely by variation in secondary structure. (doi: 10.1002/pep2.24110 )