Abstract
The design of peptide-based therapeutics is generally based on the replacement ofl-amino acids withd-isomers to obtain improved therapeutic efficiency. However,d-isomers are expensive and frequently induce undesirable immune responses. In the present work, we demonstrate that an intra-mitochondrially self-assembling amphiphilic peptide exhibits analogous activity in bothd- andl-isomeric forms. This outcome is in contrast to the general observation considering higher therapeutic efficiencies ofd-isomers compared withl-analogues. This suggests thatl-peptides overcome proteolytic degradation during intra-mitochondrial self-assembly bothin vitroandin vivo.
Original language | English |
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Pages (from-to) | 6265-6268 |
Number of pages | 4 |
Journal | Chemical Communications |
Volume | 56 |
Issue number | 46 |
DOIs | |
Publication status | Published - 2020 Jun 11 |
ASJC Scopus subject areas
- Catalysis
- Electronic, Optical and Magnetic Materials
- Ceramics and Composites
- Chemistry(all)
- Surfaces, Coatings and Films
- Metals and Alloys
- Materials Chemistry