Ions Modulate Key Interactions between pHLIP and Lipid Membranes.


Journal

Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626

Informations de publication

Date de publication:
03 09 2019
Historique:
received: 20 03 2019
revised: 05 07 2019
accepted: 22 07 2019
pubmed: 20 8 2019
medline: 17 9 2020
entrez: 20 8 2019
Statut: ppublish

Résumé

The pH-low insertion peptide (pHLIP) is used for targeted delivery of drug cargoes to acidic tissues such as tumors. The extracellular acidosis found in solid tumors triggers pHLIP to transition from a membrane-adsorbed state to fold into a transmembrane α-helix. Different factors influence the acidity required for pHLIP to insert into lipid membranes. One of them is the lipid headgroup composition, which defines the electrostatic profile of the membrane. However, the molecular interactions that drive the adsorption of pHLIP to the bilayer surface are poorly understood. In this study, we combine biophysical experiments and all-atom molecular dynamics simulations to understand the role played by electrostatics in the interaction between pHLIP and a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine bilayer. We observed that the solution ionic strength affects the structure of pHLIP at the membrane surface as well as the acidity needed for different steps in the membrane insertion process. In particular, our simulations revealed that an increase in ionic strength affected both pHLIP and the bilayer; the coordination of sodium ions with the C-terminus of pHLIP led to localized changes in helicity, whereas the coordination of sodium ions with the phosphate moiety of the phosphocholine headgroups had a condensing effect on our model bilayer. These results are relevant to our understanding of environmental influences on the ability of pHLIP to adsorb to the cell membrane and are useful in our fundamental understanding of the absorption of pH-responsive peptides and cell-penetrating peptides.

Identifiants

pubmed: 31422821
pii: S0006-3495(19)30623-X
doi: 10.1016/j.bpj.2019.07.034
pmc: PMC6731387
pii:
doi:

Substances chimiques

Ions 0
Membrane Lipids 0
Membrane Proteins 0
Phosphatidylcholines 0
pHLIP protein 0
Sodium Chloride 451W47IQ8X
1-palmitoyl-2-oleoylphosphatidylcholine TE895536Y5

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

920-929

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM120642
Pays : United States
Organisme : NIGMS NIH HHS
ID : R15 GM120676
Pays : United States

Commentaires et corrections

Type : CommentIn

Informations de copyright

Copyright © 2019 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Auteurs

Justin Westerfield (J)

Department of Biochemistry & Cellular and Molecular Biology, University of Tennessee-Knoxville, Knoxville, Tennessee.

Chitrak Gupta (C)

C. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, West Virginia.

Haden L Scott (HL)

Department of Biochemistry & Cellular and Molecular Biology, University of Tennessee-Knoxville, Knoxville, Tennessee.

Yujie Ye (Y)

Department of Biochemistry & Cellular and Molecular Biology, University of Tennessee-Knoxville, Knoxville, Tennessee.

Alayna Cameron (A)

Department of Biochemistry & Cellular and Molecular Biology, University of Tennessee-Knoxville, Knoxville, Tennessee.

Blake Mertz (B)

C. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, West Virginia; WVU Cancer Institute, West Virginia University, Morgantown, West Virginia. Electronic address: blake.mertz@mail.wvu.edu.

Francisco N Barrera (FN)

Department of Biochemistry & Cellular and Molecular Biology, University of Tennessee-Knoxville, Knoxville, Tennessee. Electronic address: fbarrera@utk.edu.

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Classifications MeSH