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Intra-mitochondrial self-assembly to overcome the intracellular enzymatic degradation of l-peptides

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Abstract

The design of peptide-based therapeutics is generally based on the replacement of L-amino acids with D-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 both D- and L-isomeric forms. This outcome is in contrast to the general observation considering higher therapeutic efficiencies of D-isomers compared with L-analogues. This suggests that L-peptides overcome proteolytic degradation during intra-mitochondrial self-assembly both in vitro and in vivo.

Graphical abstract: Intra-mitochondrial self-assembly to overcome the intracellular enzymatic degradation of l-peptides

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Supplementary files

Article information


Submitted
18 Mar 2020
Accepted
15 Apr 2020
First published
16 Apr 2020

Chem. Commun., 2020, Advance Article
Article type
Communication

Intra-mitochondrial self-assembly to overcome the intracellular enzymatic degradation of L-peptides

M. T. Jeena, S. Lee, A. K. Barui, S. Jin, Y. Cho, S. Hwang, S. Kim and J. Ryu, Chem. Commun., 2020, Advance Article , DOI: 10.1039/D0CC02029J

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