| Literature DB >> 26046483 |
Joshua Schwochert1, Rushia Turner1, Melissa Thang1, Ray F Berkeley1, Alexandra R Ponkey1, Kelsie M Rodriguez1, Siegfried S F Leung2, Bhagyashree Khunte3, Gilles Goetz3, Chris Limberakis3, Amit S Kalgutkar4, Heather Eng5, Michael J Shapiro3, Alan M Mathiowetz6, David A Price6, Spiros Liras6, Matthew P Jacobson2, R Scott Lokey1.
Abstract
The effect of peptide-to-peptoid substitutions on the passive membrane permeability of an N-methylated cyclic hexapeptide is examined. In general, substitutions maintained permeability but increased conformational heterogeneity. Diversification with nonproteinogenic side chains increased permeability up to 3-fold. Additionally, the conformational impact of peptoid substitutions within a β-turn are explored. Based on these results, the strategic incorporation of peptoid residues into cyclic peptides can maintain or improve cell permeability, while increasing access to diverse side-chain functionality.Mesh：
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Year: 2015 PMID： 26046483 DOI： 10.1021/acs.orglett.5b01162
Source DB: PubMed Journal: Org Lett ISSN： 1523-7052 Impact factor: 6.005