Evidence map›Paper›PMID 22403024›Full record

ArticlePharmaceutical research2012

Protein encapsulation in unilamellar liposomes: high encapsulation efficiency and a novel technique to assess lipid-protein interaction.

Xiaoming Xu, Antonio Costa, Diane J Burgess

Abstract read
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In one paragraph

Article in Pharmaceutical research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

41 citing papers in PubMed, 110 citations in OpenAlex.

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  8. Development and Characterization ofAntioxidants (Basel, Switzerland) · 2023
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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

3 authors at 1 institution in 1 country.

Xiaoming XuDepartment of Pharmaceutical Sciences, University of Connecticut, 69 N Eagleville Rd U3092, Storrs, Connecticut 06269, USA.
Antonio Costa
Diane J Burgess
University of Connecticut · US

Funding

PHS HHS HHSF223201011124P
6 · The paper itself

Abstract

purposeTo encapsulate a large amount of protein (superoxide dismutase, SOD) into unilamellar liposomes using a simple process and to investigate the lipid-protein interaction.

methodTo achieve protein encapsulation, preformed unilamellar empty liposomes were mixed with SOD and subjected to freeze-thaw cycling. To investigate the lipid-protein interaction, a novel light scattering technique was used.

resultsUp to 50% protein encapsulation was achieved at ∼150 nm. There was no significant change in particle size following the freeze-thaw cycling. SOD had a strong interaction with DPPC liposomes containing high concentration of cholesterol. Light scattering data revealed that in some cases the SOD molecules were present inside the lipid bilayer.

conclusionsThe method reported here allows great flexibility in the manufacturing process as the liposome preparation and protein-loading operations can be separated. Accordingly, empty liposomes can be prepared without concern about protein stability, making the manufacturing process more flexible and easy to control and ultimately leading to improved product quality. To explain the SOD-lipid interaction, a "pocket-embedding" theory was proposed. The encapsulation method reported here can be applied to hydrophilic small molecules as well as most hydrophilic proteins to achieve high encapsulation efficiency.

Indexed as

AnimalsCattleCholesterolFreezingLightLipid MetabolismLipidsParticle SizeScattering, RadiationSuperoxide DismutaseUnilamellar LiposomesCholesterolLipidsSuperoxide DismutaseUnilamellar Liposomes

Identifiers

PMID22403024
OpenAlexW2073080582

What OpenQuestion holds

Textmetadata
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.