Evidence map›Paper›PMID 40173326›Full record

ArticleBiomacromolecules2025

Preparation, Conformational Structure, and Proteolytic Activity of Papain Covalently Conjugated to Poly(ethylene glycol)-Tethered Lipid Bilayer Membranes.

Yuya Takahashi, Kyohei Kubota, Makoto Yoshimoto, Noriko Yoshimoto

Abstract read
In one paragraph

Article in Biomacromolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Article
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

4 authors.

Yuya TakahashiDepartment of Applied Chemistry, Yamaguchi University, Tokiwadai 2-16-1, Ube 755-8611, Japan.
Kyohei KubotaDepartment of Applied Chemistry, Yamaguchi University, Tokiwadai 2-16-1, Ube 755-8611, Japan.
Makoto YoshimotoDepartment of Applied Chemistry, Yamaguchi University, Tokiwadai 2-16-1, Ube 755-8611, Japan.ORCID 0000-0001-7489-229X
Noriko YoshimotoDepartment of Applied Chemistry, Yamaguchi University, Tokiwadai 2-16-1, Ube 755-8611, Japan.ORCID 0000-0002-3171-9953

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Conjugation of enzymes to lipid membranes is a key approach to reconstitute fascinating features of cell organelles and to deduce the nature of membrane-involved biological events. In this work, papain was covalently conjugated via a cross-linker to phospholipid vesicles (liposomes) tethered with poly(ethylene glycol) (PEG) at 25 °C and pH = 7.0, followed by chromatographic purification. The size of the PEG moiety and the type of cross-linker were optimized to obtain PEG-tethered liposome-conjugated papain (liposome-PEG-papain). Slight conformational changes of the membrane-conjugated papain in both its secondary and tertiary structures were revealed using circular dichroism and intrinsic fluorescence measurements. Notably, heat treatment of a liposome-PEG-papain dispersion at 77 or 84 °C caused permeabilization of the lipid membranes to 5(6)-carboxyfluorescein. Furthermore, liposome-PEG-papain exhibited the digestion activity of casein at 37 °C and pH = 7.6. The structural flexibility of liposomes as enzyme carriers may provide the opportunity to functionalize the membrane-conjugated biomacromolecules.

Indexed as

Lipid BilayersPapainPolyethylene GlycolsCircular DichroismLiposomesProtein ConformationProteolysisLipid BilayersLiposomesPapainPolyethylene Glycols

Identifiers

PMID40173326
PMCPMC12004522

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.