Membrane Active Peptides Remove Surface Adsorbed Protein Corona From Extracellular Vesicles of Red Blood Cells.

antimicrobial peptide biomembrane extracellular vesicles liposome protein corona

Journal

Frontiers in chemistry
ISSN: 2296-2646
Titre abrégé: Front Chem
Pays: Switzerland
ID NLM: 101627988

Informations de publication

Date de publication:
2020
Historique:
received: 27 05 2020
accepted: 07 07 2020
entrez: 28 8 2020
pubmed: 28 8 2020
medline: 28 8 2020
Statut: epublish

Résumé

Besides the outstanding potential in biomedical applications, extracellular vesicles (EVs) are also promising candidates to expand our knowledge on interactions between vesicular surface proteins and small-molecules which exert biomembrane-related functions. Here we provide mechanistic details on interactions between membrane active peptides with antimicrobial effect (MAPs) and red blood cell derived EVs (REVs) and we demonstrate that they have the capacity to remove members of the protein corona from REVs even at lower than 5 μM concentrations. In case of REVs, the Soret-band arising from the membrane associated hemoglobins allowed to follow the detachment process by flow-Linear Dichroism (flow-LD). Further on, the significant change on the vesicle surfaces was confirmed by transmission electron microscopy (TEM). Since membrane active peptides, such as melittin have the affinity to disrupt vesicles, a combination of techniques, fluorescent antibody labeling, microfluidic resistive pulse sensing, and flow-LD were employed to distinguish between membrane destruction and surface protein detachment. The removal of protein corona members is a newly identified role for the investigated peptides, which indicates complexity of their

Identifiants

pubmed: 32850685
doi: 10.3389/fchem.2020.00703
pmc: PMC7432246
doi:

Types de publication

Journal Article

Langues

eng

Pagination

703

Informations de copyright

Copyright © 2020 Singh, Szigyártó, Ricci, Zsila, Juhász, Mihály, Bősze, Bulyáki, Kardos, Kitka, Varga and Beke-Somfai.

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Auteurs

Priyanka Singh (P)

Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, Hungary.

Imola Cs Szigyártó (IC)

Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, Hungary.

Maria Ricci (M)

Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, Hungary.

Ferenc Zsila (F)

Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, Hungary.

Tünde Juhász (T)

Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, Hungary.

Judith Mihály (J)

Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, Hungary.

Szilvia Bősze (S)

MTA-ELTE Research Group of Peptide Chemistry, Eötvös Loránd University, Budapest, Hungary.

Éva Bulyáki (É)

Department of Biochemistry, Institute of Biology, Eötvös Loránd University, Budapest, Hungary.

József Kardos (J)

Department of Biochemistry, Institute of Biology, Eötvös Loránd University, Budapest, Hungary.

Diána Kitka (D)

Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, Hungary.

Zoltán Varga (Z)

Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, Hungary.

Tamás Beke-Somfai (T)

Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, Hungary.

Classifications MeSH