Evidence map›Paper›PMID 37242715›Full record

ArticlePharmaceutics2023

Nano Differential Scanning Fluorimetry as a Rapid Stability Assessment Tool in the Nanoformulation of Proteins.

Sofia Lisina, Wali Inam, Mikko Huhtala, Fadak Howaili, Hongbo Zhang, Jessica M Rosenholm

Open access · goldAbstract read
In one paragraph

Article in Pharmaceutics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
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

6 citing papers in PubMed, 15 citations in OpenAlex.

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  3. Review
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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

6 authors at 1 institution in 1 country.

Sofia LisinaPharmaceutical Sciences Laboratory, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland.ORCID 0009-0008-7919-216X
Wali InamPharmaceutical Sciences Laboratory, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland.
Mikko HuhtalaStructural Bioinformatics Laboratory, Faculty of Science and Engineering, Biochemistry, Åbo Akademi University, 20500 Turku, Finland.ORCID 0000-0001-6070-7604
Fadak HowailiPharmaceutical Sciences Laboratory, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland.
Hongbo ZhangPharmaceutical Sciences Laboratory, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland.ORCID 0000-0002-1071-4416
Jessica M RosenholmPharmaceutical Sciences Laboratory, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland.ORCID 0000-0001-6085-1112
Åbo Akademi University · FI

Funding

Finnish National Agency for Education TM-19-11208Finnish Pharmaceutical Society (to S.L.)Magnus Ehrnrooth Foundation (to J.M.R.)Sigrid Jusélius Foundation (to J.M.R.)
6 · The paper itself

Abstract

The development and production of innovative protein-based therapeutics is a complex and challenging avenue. External conditions such as buffers, solvents, pH, salts, polymers, surfactants, and nanoparticles may affect the stability and integrity of proteins during formulation. In this study, poly (ethylene imine) (PEI) functionalized mesoporous silica nanoparticles (MSNs) were used as a carrier for the model protein bovine serum albumin (BSA). To protect the protein inside MSNs after loading, polymeric encapsulation with poly (sodium 4-styrenesulfonate) (NaPSS) was used to seal the pores. Nano differential scanning fluorimetry (NanoDSF) was used to assess protein thermal stability during the formulation process. The MSN-PEI carrier matrix or conditions used did not destabilize the protein during loading, but the coating polymer NaPSS was incompatible with the NanoDSF technique due to autofluorescence. Thus, another pH-responsive polymer, spermine-modified acetylated dextran (SpAcDEX), was applied as a second coating after NaPSS. It possessed low autofluorescence and was successfully evaluated with the NanoDSF method. Circular dichroism (CD) spectroscopy was used to determine protein integrity in the case of interfering polymers such as NaPSS. Despite this limitation, NanoDSF was found to be a feasible and rapid tool to monitor protein stability during all steps needed to create a viable nanocarrier system for protein delivery.

Indexed as

bovine serum albuminmesoporous silica nanoparticlesmicrofluidicsnano differential scanning fluorimetryprotein encapsulationprotein stability

Identifiers

PMID37242715
PMCPMC10223687
OpenAlexW4376280140

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.