Evidence map›Paper›PMID 41727055›Full record

ArticlebioRxiv : the preprint server for biology2026

Investigation of Regulation and Binding Patterns of the Human Cathelicidin Peptide LL-37 in Complexation with Nucleic Acids, and its Impact on Neutrophil Extracellular Traps.

Claudia Zielke, Behzad Rad, Josefine E Nielsen, Jiaxin Li, Sopida Pimcharoen, Manasi Sawant, Jennifer S Lin, Hawa R Thiam, Annelise E Barron

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Claudia ZielkeDepartment of Bioengineering, Stanford University, Schools of Medicine and of Engineering, Stanford, California 94305, USA.
Behzad RadMolecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Josefine E NielsenDepartment of Bioengineering, Stanford University, Schools of Medicine and of Engineering, Stanford, California 94305, USA.
Jiaxin LiDepartment of Bioengineering, Stanford University, Schools of Medicine and of Engineering, Stanford, California 94305, USA.
Sopida PimcharoenDepartment of Bioengineering, Stanford University, Schools of Medicine and of Engineering, Stanford, California 94305, USA.
Manasi SawantDepartment of Bioengineering, Stanford University, Schools of Medicine and of Engineering, Stanford, California 94305, USA.
Jennifer S LinDepartment of Bioengineering, Stanford University, Schools of Medicine and of Engineering, Stanford, California 94305, USA.
Hawa R ThiamDepartment of Bioengineering, Stanford University, Schools of Medicine and of Engineering, Stanford, California 94305, USA.
Annelise E BarronDepartment of Bioengineering, Stanford University, Schools of Medicine and of Engineering, Stanford, California 94305, USA.

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Aina E. Cohen, KEITH O HODGSON · 2020 to 2026
$43.3M
NIGMS NIH HHS P30 GM133894
6 · The paper itself

Abstract

The human cathelicidin host defense peptide LL-37 forms complexes with nucleic acids that can have either beneficial or detrimental health effects. We suggest that these differential impacts are directly connected to dsDNA binding by LL-37 and to complex formation between protomers. Here, we show using phage λ DNA that LL-37 binds non-specifically to dsDNA, condensing it, followed by complex formation between LL-37 peptides. We find that complex formation is concentration-dependent, with low LL-37 amounts yielding loosely aggregated DNA structures, while higher LL-37 concentrations lead to well-defined, disc-like structures of about 150 nm in diameter. The condensation of the nucleic acids, which causes a loss of the characteristic B-DNA features, results from interactions of the phosphodiester backbone with protonated amino acid side chains of the peptide at physiological pH, predominantly in A-T rich sequences of the nucleic acid. However, in our studies, electrostatic interactions did not appear to be the driving force for complexation, but rather we found the α-helical structure of the peptide with its amphipathic and hydrophobic surfaces to be essential. Further, we show that LL-37 also interacts with nucleic acids from neutrophil extracellular traps (NETs) in a concentration-dependent way, causing a reduction in NET aggregate area, which may offer new biophysical insights into diseases such as systemic lupus erythematosus (SLE), which involve slower-than-normal NET clearance. Our results indicate the key importance of LL-37 expression levels for regulation of the innate immune system for optimal human health, since the relative amounts of expressed LL-37 present to interact with extracellular DNA will determine the extent to which the DNA can be condensed, which in turn will affect the ability of the body to clear the NETs before they can cause inflammatory conditions.

Indexed as

antimicrobial peptidecondensationinnate immunityintermolecular interactionslambda DNALL-37neutrophils

Identifiers

PMID41727055
PMCPMC12918999

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.