ArticleNature communications2026
A modular self-assembling peptide platform targeting TGF-β1 for tendon regeneration.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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10 authors.
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Abstract
Excessive transforming growth factor-β1 (TGF-β1) signaling is a key driver of the pathological processes of fibrosis and matrix disorganization in tendinopathy, yet current treatments do not directly target this fibrotic microenvironment. Here we show that a self-assembling peptide composed entirely of natural amino acids, AsPep-FTSQ, can locally capture TGF-β1 and remodel the pathological tendon niche. Injecting AsPep-FTSQ into rat and beagle models of tendinopathy resulted in the formation of an interconnected nanofibrous network in situ that selectively sequesters excess TGF-β1. This network suppresses pro-fibrotic signaling, limits pathological tendon cell (TC) state transitions, and promotes collagen realignment. These effects improve tendon structure and functional repair across species. This fully natural, self-assembling peptide composed of amino acids provides a modular strategy for local cytokine sequestration and suggests a therapeutic approach for tendinopathy and potentially other fibrotic soft-tissue disorders.
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