Amphipathic Proline-Rich Cell Penetrating Peptides for Targeting Mitochondria

Cell-penetrating peptides (CPPs) offer a platform for targeted intracellular delivery. Here, we developed amphipathic oligoprolines for targeting mitochondria. The rigid peptides feature cationic guanidinium and hydrophobic cyclohexyl groups aligned along the edges of the polyproline II (PPII) helical backbone. Systematic variations of the hydrophobicity through C-terminal and backbone modifications provided CPPs with enhanced cellular uptake and mitochondrial selectivity. Comparative studies with conformationally more flexible analogs revealed the benefit of aligned cationic and hydrophobic residues on a rigid backbone for mitochondria targeting. Notably, the amphipathic peptides undergo time-dependent intracellular redistribution, leading to selective and prolonged mitochondrial residency. Our findings established design principles for optimizing CPPs to target mitochondria.

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Publication Details

Journal
ACS Chemical Biology
Published
2025-08-19
DOI
https://doi.org/10.1021/acschembio.5c00479
Citations
3
Primary Topic
RNA Interference and Gene Delivery
Type
article
Field-Weighted Citation Impact
2.42

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article

Amphipathic Proline-Rich Cell Penetrating Peptides for Targeting Mitochondria

Helma Wennemers, Adeline Marie Schmitt
3 citations
ACS Chemical Biology
RNA Interference and Gene Delivery
2.42
article

Amphipathic Proline-Rich Cell Penetrating Peptides for Targeting Mitochondria

Helma Wennemers, Adeline Marie Schmitt
article en
3 citations

Abstract

Cell-penetrating peptides (CPPs) offer a platform for targeted intracellular delivery. Here, we developed amphipathic oligoprolines for targeting mitochondria. The rigid peptides feature cationic guanidinium and hydrophobic cyclohexyl groups aligned along the edges of the polyproline II (PPII) helical backbone. Systematic variations of the hydrophobicity through C-terminal and backbone modifications provided CPPs with enhanced cellular uptake and mitochondrial selectivity. Comparative studies with conformationally more flexible analogs revealed the benefit of aligned cationic and hydrophobic residues on a rigid backbone for mitochondria targeting. Notably, the amphipathic peptides undergo time-dependent intracellular redistribution, leading to selective and prolonged mitochondrial residency. Our findings established design principles for optimizing CPPs to target mitochondria.

ACS Chemical BiologyVol. 20(9)
ETH Zurich (CH)
Eidgenössische Technische Hochschule Zürich
Openalex Percentile: Top 11%
RNA Interference and Gene Delivery
2.42
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Amphipathic Proline-Rich Cell Penetrating Peptides for Targeting Mitochondria — Helma Wennemers, Adeline Marie Schmitt · ACS Chemical Biology (2025) | TGRS Research Map | TGRS