Journal
MOLECULES
Volume 28, Issue 2, Pages -Publisher
MDPI
DOI: 10.3390/molecules28020780
Keywords
synthesis; helix mimetics; protein-protein interactions; PCNA
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A novel hydrogen bond surrogate-based alpha-helix mimetic was designed using covalent H-bond replacement and an ether linkage to substitute an amide bond. CD studies showed that the mimetic maintained stable conformations in aqueous buffer at high temperatures.
A novel hydrogen bond surrogate-based (HBS) alpha-helix mimetic was designed by the combination of covalent H-bond replacement and the use of an ether linkage to substitute an amide bond within a short peptide sequence. The new helix template could be placed in position other than the N-terminus of a short peptide, and the CD studies demonstrate that the template adopts stable conformations in aqueous buffer at exceptionally high temperatures.
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