ArticleJACS Au2026
Heteroaggregation of Antimicrobial Peptides LL-37 and HNP‑1 Drives Cooperative Neutralization of Cytotoxicity.
Article in JACS Au, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
- Apoptosis Modulation by LL-37: From Mitochondrial Cell Death to Prosurvival Signaling.International journal of molecular sciences · 2026Review
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Synergistic bactericidal effects between antimicrobial peptides (AMPs) have been widely studied, yet their cooperative roles in reducing host-cell cytotoxicity remain poorly understood. Inspired by the cross-seeding observed in α-synuclein and β-amyloid fibril formation, we report that the cooperative reduction of cytotoxicity by two major AMPs, human cathelicidin (LL-37) and human α-defensin-1 (HNP-1), is governed by their heteroaggregation states. Through the integration of dynamic light scattering (DLS), MTT assays, Fluo-3 calcium imaging, live/dead staining, apoptosis/necrosis assays, ROS detection (DCFH-DA), and both optical and atomic force microscopy, we demonstrate that the neutralization of MDCK-I cytotoxicity occurs only at a stoichiometric ratio of HNP-1 to LL-37 of approximately 0.025. Furthermore, the observed loss of function results from mutual antagonism: HNP-1 suppresses LL-37-induced necrosis, while LL-37 reduces the level of HNP-1-induced apoptosis. These findings highlight peptide aggregation as a critical determinant of AMP structure-function relationships.
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