Evidence map›Paper›PMID 38766164›Full record

ArticlebioRxiv : the preprint server for biology2024

Polymer-tethered quenched fluorescent probes for enhanced imaging of tumor associated proteases.

Martin Hadzima, Franco Faucher, Kristýna Blažková, Joshua J Yim, Matteo Guerra, Shiyu Chen, Emily C Woods, Ki Wan Park, Pavel Šácha, Vladimír Šubr and 5 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2024. 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

5 · Who and what money

Authors and funding

15 authors.

Martin HadzimaInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 16610, Praha 6, Czech Republic.
Franco FaucherDepartment of Chemistry, Stanford University, Stanford, California, 94305, United States.
Kristýna BlažkováDepartment of Pathology, School of Medicine, Stanford University, Stanford, California, 94305, United States.
Joshua J YimDepartment of Pathology, School of Medicine, Stanford University, Stanford, California, 94305, United States.
Matteo GuerraDepartment of Pathology, School of Medicine, Stanford University, Stanford, California, 94305, United States.
Shiyu ChenDepartment of Pathology, School of Medicine, Stanford University, Stanford, California, 94305, United States.
Emily C WoodsDepartment of Pathology, School of Medicine, Stanford University, Stanford, California, 94305, United States.
Ki Wan ParkDepartment of Pathology, School of Medicine, Stanford University, Stanford, California, 94305, United States.
Pavel ŠáchaInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 16610, Praha 6, Czech Republic.
Vladimír ŠubrInstitute of Macromolecular Chemistry, Czech Academy of Sciences, Heyrovského n. 2, 16206, Praha 6, Czech Republic.
Libor KostkaInstitute of Macromolecular Chemistry, Czech Academy of Sciences, Heyrovského n. 2, 16206, Praha 6, Czech Republic.
Tomáš EtrychInstitute of Macromolecular Chemistry, Czech Academy of Sciences, Heyrovského n. 2, 16206, Praha 6, Czech Republic.
Pavel MajerInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 16610, Praha 6, Czech Republic.
Jan KonvalinkaInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 16610, Praha 6, Czech Republic.
Matthew BogyoDepartment of Pathology, School of Medicine, Stanford University, Stanford, California, 94305, United States.ORCID 0000-0003-3753-4412

Funding

Dual orthogonal fluorescent protease sensors for image guided surgeryR01EB028628 · NIBIB · STANFORD UNIVERSITY · PI BOGYO, MATTHEW · 2019 to 2023
$1.9M
NIBIB NIH HHS R01 EB028628
6 · The paper itself

Abstract

Fluorescence-based contrast agents enable real-time detection of solid tumors and their neovasculature, making them ideal for use in image-guided surgery. Several agents have entered late-stage clinical trials or secured FDA approval, suggesting they are likely to become standard of care in cancer surgeries. One of the key parameters to optimize in contrast agent is molecular size, which dictates much of the pharmacokinetic and pharmacodynamic properties of the agent. Here, we describe the development of a class of protease-activated quenched fluorescent probes in which a N-(2-hydroxypropyl)methacrylamide copolymer is used as the primary scaffold. This copolymer core provides a high degree of probe modularity to generate structures that cannot be achieved with small molecules and peptide probes. We used a previously validated cathepsin substrate and evaluated the effects of length and type of linker as well as positioning of the fluorophore/quencher pair on the polymer core. We found that the polymeric probes could be optimized to achieve increased over-all signal and tumor-to-background ratios compared to the reference small molecule probe. Our results also revealed multiple structure-activity relationship trends that can be used to design and optimize future optical imaging probes. Furthermore, they confirm that a hydrophilic polymer is an ideal scaffold for use in optical imaging contrast probes, allowing a highly modular design that enables efficient optimization to maximize probe accumulation and overall biodistribution properties.

Indexed as

cancerfluorescenceHPMA copolymeriBodyimagingprotease

Identifiers

PMID38766164
PMCPMC11100723

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.