Evidence map›Paper›PMID 36107722›Full record

ArticleAnalytical chemistry2022

Solid-to-Liposome Conformational Transition of Phosphatidylcholine and Phosphatidylserine Probed by Atomic Force Microscopy, Infrared Spectroscopy, and Density Functional Theory Calculations.

Tianyi Dou, Clara Zens, Katrin Schröder, Yuan Jiang, Alexey A Makarov, Stephan Kupfer, Dmitry Kurouski

Abstract read
In one paragraph

Article in Analytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

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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

7 authors.

Tianyi DouDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States.
Clara ZensInstitute of Physical Chemistry, Friedrich Schiller University Jena, Helmholtzweg 4, 07743 Jena, Germany.
Katrin SchröderInstitute of Physical Chemistry, Friedrich Schiller University Jena, Helmholtzweg 4, 07743 Jena, Germany.
Yuan JiangMerck & Company Inc., MRL, Analytical Research & Development, Boston, Massachusetts 02115, United States.ORCID 0000-0002-2997-9297
Alexey A MakarovMerck & Company Inc., MRL, Analytical Research & Development, Boston, Massachusetts 02115, United States.ORCID 0000-0003-4866-0430
Stephan KupferInstitute of Physical Chemistry, Friedrich Schiller University Jena, Helmholtzweg 4, 07743 Jena, Germany.ORCID 0000-0002-6428-7528
Dmitry KurouskiDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States.ORCID 0000-0002-6040-4213

Funding

Biophysical determination of the underlying cause of α-Syn oligomer toxicityR35GM142869 · NIGMS · TEXAS A&M AGRILIFE RESEARCH · PI KUROUSKI, DMITRY · 2021 to 2025
$1.6M
NIGMS NIH HHS R35 GM142869
6 · The paper itself

Abstract

Liposomes are emerging therapeutic formulations for site-specific delivery of chemotherapeutic drugs. The efficiency and selectivity of drug delivery by these carriers largely rely on their surface properties, shape, and size. There is a growing demand for analytical approaches that can be used for structural and morphological characterization of liposomes at the single-vesicle level. AFM-IR is a modern optical nanoscopic technique that combines the advantages of scanning probe microscopy and infrared spectroscopy. Our findings show that AFM-IR can be used to probe conformational changes in phospholipids that take place upon their assembly into liposomes. Such conclusions can be made based on the corresponding changes in intensities of the lipid vibrational bands as the molecules transition from a solid state into large unilamellar vesicles (LUVs). This spectroscopic analysis of LUV formation together with density functional theory calculations also reveals the extent to which the molecular conformation and local environment of the functional groups alter the AFM-IR spectra of phospholipids. Using melittin as a test protein, we also examined the extent to which LUVs can be used for protein internalization. We found that melittin enters LUVs nearly instantaneously, which protects it from possible structural modifications that are caused by a changing environment. This foundational work empowers AFM-IR analysis of liposomes and opens new avenues for determination of the molecular mechanisms of liposome-drug interactions.

Indexed as

LiposomesPhosphatidylcholinesDensity Functional TheoryMelittenMicroscopy, Atomic ForceMolecular ConformationPhosphatidylserinesPhospholipidsSpectrophotometry, InfraredUnilamellar LiposomesLiposomesMelittenPhosphatidylcholinesPhosphatidylserinesPhospholipidsUnilamellar Liposomes

Identifiers

PMID36107722
PMCPMC10405298

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Registered trials

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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.