Evidence map›Paper›PMID 40222963›Full record

ArticleAngewandte Chemie (International ed. in English)2025

Conformationally Locked Peptide-DNA Nanostructures for CRISPR-Amplified Activity-Based Sensing.

Dylan M Snider, Mackenzie L Coffin, Brian J Armijo, Ryan Khetan, Mark W Duchow, Anna Capasso, Devleena Samanta

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed, 1 pooled it
–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

4 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Review
  4. Article
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

7 authors.

Dylan M SniderDepartment of Chemistry, The University of Texas at Austin, 105 E 24th St., Austin, TX 78712, USA.
Mackenzie L CoffinDepartment of Chemistry, The University of Texas at Austin, 105 E 24th St., Austin, TX 78712, USA.
Brian J ArmijoDepartment of Chemistry, The University of Texas at Austin, 105 E 24th St., Austin, TX 78712, USA.
Ryan KhetanDepartment of Chemistry, The University of Texas at Austin, 105 E 24th St., Austin, TX 78712, USA.
Mark W DuchowDepartment of Oncology, Dell Medical School, The University of Texas at Austin, 1601 Trinity St., Austin, TX 78712, USA.
Anna CapassoDepartment of Oncology, Dell Medical School, The University of Texas at Austin, 1601 Trinity St., Austin, TX 78712, USA.
Devleena SamantaDepartment of Chemistry, The University of Texas at Austin, 105 E 24th St., Austin, TX 78712, USA.

Funding

American Cancer Society IRG-21-135-01-IRGCancer Prevention and Research Institute of Texas RR 160093David and Lucile Packard Foundation 2024-77398National Science Foundation CHE 2404334
6 · The paper itself

Abstract

We introduce a new class of chemical probes for activity-based sensing of proteases, termed cleavable, locked initiator probes (CLIPs). CLIPs contain a protease-cleavable peptide linked between two programmable DNA strands-an "initiator" DNA and a shorter "blocking" DNA. These DNA sequences are designed to hybridize, creating a "locked" hairpin-like structure. Upon proteolytic cleavage, the initiator strand is released, triggering the activation of CRISPR-Cas12a enzymes and producing an amplified fluorescence response. CLIPs generate more than 20-fold turn-on signals at room temperature (25 °C), significantly outperforming commercial probes by yielding ∼40-fold lower limits of detection (LOD) at 100-fold lower concentrations. Their versatility enables the detection of various disease-relevant proteases-including the SARS-CoV-2 main protease, caspase-3, matrix metalloproteinase-7, and cathepsin B-simply by altering the peptide sequence. Importantly, CLIPs detect cathepsin B in four different colorectal cancer cell lines, highlighting their clinical potential. Taken together, the sensitivity (LOD: ∼88 pM), selectivity, and rapid assay time (down to 35 min), combined with the ability to operate in complex biological media with minimal sample preparation, position CLIPs as powerful chemical tools for activity-based sensing of functional enzymes.

Indexed as

Biosensing TechniquesCRISPR-Cas SystemsDNANanostructuresPeptidesCaspase 3Cathepsin BHumansLimit of DetectionMatrix Metalloproteinase 7SARS-CoV-2Caspase 3Cathepsin BDNAMatrix Metalloproteinase 7PeptidesActivity‐based sensingDetectionDNANanostructuresProtease

Identifiers

PMID40222963
PMCPMC12171325

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.