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

M. T. Jeena; Seokyoung Lee; Ayan Kumar Barui; Seongeon Jin; Yuri Cho; Suk Won Hwang; Sehoon Kim; Ja Hyoung Ryu

doi:10.1039/d0cc02029j

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

M. T. Jeena, Seokyoung Lee, Ayan Kumar Barui, Seongeon Jin, Yuri Cho, Suk Won Hwang, Sehoon Kim, Ja Hyoung Ryu

Research output: Contribution to journal › Article › peer-review

15 Citations (Scopus)

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
Pages (from-to)	6265-6268
Number of pages	4
Journal	Chemical Communications
Volume	56
Issue number	46
DOIs	https://doi.org/10.1039/d0cc02029j
Publication status	Published - 2020 Jun 11

Bibliographical note

Funding Information:
This work was supported by the National Research Foundation of Korea (2017R1A2B4003617, 2016R1A5A1009405, 2017K1A3A1A 19071083, 2018R1E1A2A02058946, 2019R1I1A1A01062414, and 2017M3A9D8029942) and the Korea Research Institute of Standards and Science (KRISS-2018-GP2018-0018) for KIST intramural program.

Publisher Copyright:
© The Royal Society of Chemistry 2020.

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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title = "Intra-mitochondrial self-assembly to overcome the intracellular enzymatic degradation ofl-peptides",

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.",

author = "Jeena, {M. T.} and Seokyoung Lee and Barui, {Ayan Kumar} and Seongeon Jin and Yuri Cho and Hwang, {Suk Won} and Sehoon Kim and Ryu, {Ja Hyoung}",

note = "Funding Information: This work was supported by the National Research Foundation of Korea (2017R1A2B4003617, 2016R1A5A1009405, 2017K1A3A1A 19071083, 2018R1E1A2A02058946, 2019R1I1A1A01062414, and 2017M3A9D8029942) and the Korea Research Institute of Standards and Science (KRISS-2018-GP2018-0018) for KIST intramural program. Publisher Copyright: {\textcopyright} The Royal Society of Chemistry 2020.",

year = "2020",

month = jun,

day = "11",

doi = "10.1039/d0cc02029j",

language = "English",

volume = "56",

pages = "6265--6268",

journal = "Chemical Communications",

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publisher = "Royal Society of Chemistry",

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T1 - Intra-mitochondrial self-assembly to overcome the intracellular enzymatic degradation ofl-peptides

AU - Jeena, M. T.

AU - Lee, Seokyoung

AU - Barui, Ayan Kumar

AU - Jin, Seongeon

AU - Cho, Yuri

AU - Hwang, Suk Won

AU - Kim, Sehoon

AU - Ryu, Ja Hyoung

N1 - Funding Information: This work was supported by the National Research Foundation of Korea (2017R1A2B4003617, 2016R1A5A1009405, 2017K1A3A1A 19071083, 2018R1E1A2A02058946, 2019R1I1A1A01062414, and 2017M3A9D8029942) and the Korea Research Institute of Standards and Science (KRISS-2018-GP2018-0018) for KIST intramural program. Publisher Copyright: © The Royal Society of Chemistry 2020.

PY - 2020/6/11

Y1 - 2020/6/11

N2 - 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.

AB - 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.

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U2 - 10.1039/d0cc02029j

DO - 10.1039/d0cc02029j

M3 - Article

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AN - SCOPUS:85086346489

SN - 1359-7345

VL - 56

SP - 6265

EP - 6268

JO - Chemical Communications

JF - Chemical Communications

IS - 46

ER -

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

Abstract

Bibliographical note

ASJC Scopus subject areas

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