Topology-Controlled PEGylation Enhances Renal Accumulation of Therapeutic Peptide for Treating Ischemia–Reperfusion Injury

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Authors: Yixing Wen, Z C Zhao, Xiang Zheng, Y ZHAO, Simin Sun, Shiwei Mi, Xingdi Cheng, Xueguang Lu, Qiang Wang
Cited by: 1
References: 56

Abstract

Ischemia-reperfusion injury (IRI) remains a major cause of graft dysfunction following kidney transplantation, driven in large part by mitochondrial oxidative stress and subsequent apoptotic cell death. Elamipretide (SS31), a mitochondria-targeted tetrapeptide, shows robust renoprotection in preclinical models but is constrained by rapid renal elimination and limited pharmacokinetic exposure. Here, we prepared multiarm PEG-SS31 conjugates with controlled arm number and total PEG molecular weight. A ROS-cleavable thioketal linker enabled SS31 release under oxidative stress. The lead topology self-assembles into nanoparticles, produces markedly enhanced renal accumulation relative to free SS31 and alternative architectures, and yields superior renoprotection in a murine IRI model with reduced tubular injury and apoptosis. These results identify PEG topology as a key design parameter for kidney-targeted peptide therapeutics.

Fields of Study & Subjects

Supramolecular Self-Assembly in Materials RNA Interference and Gene Delivery Cell Adhesion Molecules Research

Publication details

Journal / source
Nano Letters
Publisher
American Chemical Society (ACS)
Volume
26
Issue
26
Pages
8566–8573
Publication date
26 June 2026
Language
EN