期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1859, 期 4, 页码 577-585出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2016.08.013
关键词
Peptide; Protein-protein interaction (PPI); Transmembrane; Peptidomimetics; Lipidation; Hydrocarbon staple
资金
- Natural Science and Engineering Research Council of Canada (NSERC) [A2807]
- Canadian Institutes of Health Research [CIHR FRN-5810]
Membrane proteins play the central roles in a variety of cellular processes, ranging from nutrient uptake and signalling, to cell-cell communication. Their biological functions are directly related to how they fold and assemble; defects often lead to disease. Protein-protein interactions (PPIs) within the membrane are therefore of great interest as therapeutic targets. Here we review the progress in the application of membrane-insertable peptides for the disruption or stabilization of membrane-based PPIs. We describe the design and preparation of transmembrane peptide mimics; and of several categories of peptidomimetics used for study, including o-enantiomers, non-natural amino acids, peptoids, and beta-peptides. Further aspects of the review describe modifications to membrane-insertable peptides, including lipidation and cyclization via hydrocarbon stapling. These approaches provide a pathway toward the development of metabolically stable, non-toxic, and efficacious peptide modulators of membrane-based PPIs. This article is part of a Special Issue entitled: Lipid order/lipid defects and lipid control of protein activity edited by Dirk Schneider. (C)2016 Elsevier B.V. All rights reserved.
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