Evidence map›Paper›PMID 42450336›Full record

ArticleInternational journal of molecular sciences2026

Quantum Dots Interaction with α-Actinin via Experimental Observations and Computational Predictions.

Abhishu Chand, Elijah Billue, Tony E Astuhuaman Davila, Ridwan Sakidja, Kyoungtae Kim

Abstract read
In one paragraph

Article in International journal of molecular sciences, 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

5 authors.

Abhishu ChandDepartment of Biology, Missouri State University, 901 S National, Springfield, MO 65897, USA.
Elijah BillueDepartment of Biology, Missouri State University, 901 S National, Springfield, MO 65897, USA.ORCID 0009-0001-9090-7284
Tony E Astuhuaman DavilaDepartment of Physics, Astronomy, & Materials Science, Missouri State University, 901 S National, Springfield, MO 65897, USA.
Ridwan SakidjaDepartment of Physics, Astronomy, & Materials Science, Missouri State University, 901 S National, Springfield, MO 65897, USA.ORCID 0000-0002-6468-2376
Kyoungtae KimDepartment of Biology, Missouri State University, 901 S National, Springfield, MO 65897, USA.ORCID 0000-0003-0896-9572

Funding

Missouri State University Roy D. Blunt Life Science Professorship
6 · The paper itself

Abstract

Quantum Dots (QDs) are nanoparticles that are highly desirable for biomedical applications such as drug delivery, cellular tracking, and imaging due to their fluorescent and tunable optical properties. However, the biochemical mechanism of their interaction with intracellular proteins that regulate cytoskeletal organization remains poorly understood. While previous studies have shown QDs' ability to interact with actin and alter actin dynamics, their impacts on actin-binding proteins have not been explored. In this study, we investigated the interaction between CdSe/ZnS QDs and the actin-binding protein, α-actinin, and assessed its impact on actin cytoskeletal organization. Our results demonstrated a strong interaction between QDs and α-actinin, which impeded an α-actinin-mediated filamentous actin (F-actin) bundling, as well as compromised the activity of α-actinin in preventing actin depolymerization. Furthermore, the physics-based modeling and simulations carried out at physiological temperatures supported these findings by identifying stable interaction surfaces between QDs and α-actinin. This study provides mechanistic insight into nanoparticle-protein interactions and highlights the potential cytoskeletal toxicity associated with it.

Indexed as

ActininQuantum DotsActin CytoskeletonActinsAnimalsCadmium CompoundsHumansProtein BindingSelenium CompoundsSulfidesZinc CompoundsActininActinsCadmium Compoundscadmium selenideSelenium CompoundsSulfidesZinc Compoundszinc sulfideactin cytoskeletoncytoskeletal toxicitynanoparticle–protein interactionsphysics-based modelingquantum dotsα-actinin

Identifiers

PMID42450336
PMCPMC13362372

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.