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Inside Cover: Naturally Inspired Peptide Leads: Alanine Scanning Reveals an Actin‐Targeting Thiazole Analogue of Bisebromoamide (ChemBioChem 17/2016)
Author(s) -
Johnston Heather J.,
Boys Sarah K.,
Makda Ashraff,
Carragher Neil O.,
Hulme Alison N.
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600435
Subject(s) - alanine scanning , peptide , natural product , chemistry , thiazole , cover (algebra) , alanine , biophysics , combinatorial chemistry , biochemistry , computational biology , nanotechnology , stereochemistry , biology , materials science , amino acid , mutagenesis , gene , mechanical engineering , engineering , mutation
The inside cover picture shows an alanine‐scanning approach to exploring the structure–activity relationship of the marine cyanobacterium‐derived natural product bisebromoamide. Cell morphology assays and reverse phase protein array (RPPA) analysis have allowed the identification of a new and promising lead for use in the design of anticancer therapeutics, and as a tool to study the role of IRS‐1 expression and F‐actin aggregation. More information can be found in the full paper by A. N. Hulme et al. on page 1621 in Issue 17, 2016 (DOI: 10.1002/cbic.201600257).