Evidence map›Paper›PMID 41114157›Full record

ReviewACS omega2025

Decoding Protein Corona Through Synchrotron-Based Small-Angle X‑Ray Scattering.

Juliana Tosta Theodoro Carvalho, Antônio Malfatti-Gasperini, Ben J Boyd, Liming Wang, Mateus Borba Cardoso

Abstract readReview
In one paragraph

Review in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
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.

Juliana Tosta Theodoro CarvalhoBrazilian Synchrotron Light Laboratory (LNLS), Brazilian Center for Research in Energy and Materials (CNPEM), 13083-100 Campinas, São Paulo, Brazil.ORCID https://orcid.org/0000-0002-2834-939X
Antônio Malfatti-GasperiniBrazilian Synchrotron Light Laboratory (LNLS), Brazilian Center for Research in Energy and Materials (CNPEM), 13083-100 Campinas, São Paulo, Brazil.ORCID https://orcid.org/0000-0002-7449-5400
Ben J BoydDrug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC 3052, Australia.ORCID https://orcid.org/0000-0001-5434-590X
Liming WangCAS Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, Laboratory for Interface Science and Biology, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, P. R. China.ORCID https://orcid.org/0000-0003-1382-9195
Mateus Borba CardosoBrazilian Synchrotron Light Laboratory (LNLS), Brazilian Center for Research in Energy and Materials (CNPEM), 13083-100 Campinas, São Paulo, Brazil.ORCID https://orcid.org/0000-0003-2102-1225

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nanoparticles (NPs) in biological environments rapidly become coated with a dynamic biomolecular layer known as the protein corona (PC), significantly influencing their biological identity and functionality. Traditional methods used to characterize the PC often disrupt its native state, limiting accurate insights into its true structural and compositional complexity. Synchrotron-based small-angle X-ray scattering (SAXS) provides a powerful alternative, enabling nondestructive, label-free, and in-solution analysis of the PC under physiologically relevant conditions. This minireview critically examines recent advancements in applying SAXS to decode the PC, highlighting methodological developments and exemplary studies demonstrating SAXS's unique ability to resolve interactions at the nano-bio interface. By discussing novel analytical frameworks, such as integrating SAXS with complementary techniques like small-angle neutron scattering (SANS) and cryo-transmission electron microscopy (cryo-TEM), we provide a comprehensive overview on the structural and thermodynamic features of the PC. Furthermore, we outline future opportunities including time-resolved SAXS to elucidate the kinetics of corona formation and the establishment of standardized protocols to enhance reproducibility and reliability. Ultimately, this review positions SAXS as an indispensable tool for advancing our understanding of nanoparticle-protein interactions and fostering innovation in nanomedicine.

Identifiers

PMID41114157
PMCPMC12529176

What OpenQuestion 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 OpenQuestion graph.