# Impact of Lipid Bilayer Composition and Physicochemical Properties on Constitution of a Transmembrane Helical Peptide into Exosome-Mimetic Vesicles

https://mdr.nims.go.jp/datasets/376b5259-abe5-40e0-9132-a46392260f80

## File

- [2025MolPharm_EMV.pdf](https://mdr.nims.go.jp/filesets/9fd893c0-52bf-40b2-b871-7475b7429afc/download) ([Detail](https://mdr.nims.go.jp/filesets/9fd893c0-52bf-40b2-b871-7475b7429afc.md))

## Id

376b5259-abe5-40e0-9132-a46392260f80

## Local identifier



## Visibility

open_to_public

## State

published

## Created at

2025-11-21T09:17:54.597810Z

## Updated at

2025-11-25T03:30:04.108959Z

## Published at

2025-11-25T03:23:32.795900Z

## Doi



## First published url

https://doi.org/10.1021/acs.molpharmaceut.5c00825

## Date published

2025-11-03

## Recorded date published

2025-11-3

## Resource type

journal_article

## Manuscript type

vor

## Collection



## Title

- title: Impact of Lipid Bilayer Composition and Physicochemical Properties on Constitution
    of a Transmembrane Helical Peptide into Exosome-Mimetic Vesicles
  title_type: original
  lang: en

## Description

- description: "Exosomes are expected to efficiently deliver drugs, such as microRNAs
    and proteins, to targeted organs. However, using natural exosomes presents many
    difficulties in terms of safety, quality control, and manufacturing; therefore,
    developing exosome-mimetic artificial materials is desirable. In this study, we
    elucidated how sphingomyelin (SM) and cholesterol (CH), the\r\nmain constituents
    of the exosome membrane, in addition to phosphatidylcholine (PC), influence the
    physicochemical properties of PC vesicles. Then, the relevance of these properties
    to the secondary structure and insertion efficiency of a helical peptide, the
    transmembrane domain of integrin α, was investigated. The constitution of this
    peptide was most successful with exosome-mimetic vesicles (EMV) bearing 15 mol
    % SM and 40 mol % CH, and the exclusion of SM or CH resulted in low dispersion
    stability or\r\nunsuccessful peptide constitution. Physicochemical analysis of
    the membrane properties revealed that successful peptide incorporation into the
    lipid membrane relied on the membrane softness induced by CH and the appearance
    of a highly mobile boundary phase induced by SM, which together created a favorable
    environment for the peptide. These results provide important insights that serve
    as a foundation for developing EMV as drug carriers."
  description_type: abstract
  lang: und

## Creator

- name: Shiho Tsutsumi
  role: author
  orcid: https://orcid.org/0009-0006-8089-6477
- name: Yuki Takechi-Haraya
  role: author
  orcid: https://orcid.org/0000-0002-8754-6457
- name: Yasuhiro Abe
  role: author
  orcid: https://orcid.org/0000-0002-5931-6590
- name: Kohsaku Kawakami
  role: author
  orcid: https://orcid.org/0000-0002-3466-9365

## Contact agent



## Publisher

organization: American Chemical Society (ACS)

## Managing organization



## Keyword

- subject: Exosomes
  schema: not_defined
- subject: Exosome mimetic vesicles
  schema: not_defined
- subject: lipid membrane
  schema: not_defined
- subject: helical peptide
  schema: not_defined

## Rights

- identifier: https://creativecommons.org/licenses/by/4.0/

## Other identifier(s)



## Data origin



## Embargo



## Journal

- title: Molecular Pharmaceutics
  issn: '15438384'
  volume: '22'
  issue: '11'
  start_page: 6874
  end_page: 6886

## Conference



## Related item



## Funding

- identifier: JP23K06092
  funder_name: Japan Society for the Promotion of Science

## Instrument



## Instrument operator



## Instrument managing organization



## Measurement method



## Specimen



## Chemical composition



## Structure for specimen



## Structural feature for specimen



## Specific property for specimen



## Process for specimen treatment



## Computational method



## Energy level/transition state



## Software



## Custom property



## Fileset

- id: 9fd893c0-52bf-40b2-b871-7475b7429afc
  filename: 2025MolPharm_EMV.pdf
  content_type: application/pdf
  size: 4629855
  md5: 0c0ac600d11a3376559e1d375fa49cf7

## Thumbnail

fileset_id: 9fd893c0-52bf-40b2-b871-7475b7429afc
filename: 2025MolPharm_EMV.pdf