ArticleBiophysical journal2012
Modulation of the pHLIP transmembrane helix insertion pathway.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Membrane Composition Reshapes the Folding Landscape of a pH-Responsive Peptide.The journal of physical chemistry letters · 2026Article
- Article
- Targeted acidosis mediated delivery of antigenic MHC-binding peptides.Frontiers in immunology · 2024Article
- Aiming the magic bullet: targeted delivery of imaging and therapeutic agents to solid tumors by pHLIP peptides.Frontiers in pharmacology · 2024Review
- Arginine Residues Modulate the Membrane Interactions of pHLIP Peptides.Journal of chemical information and modeling · 2023Article
- CaProtein science : a publication of the Protein Society · 2022Article
- Pharmacokinetic modeling reveals parameters that govern tumor targeting and delivery by a pH-Low Insertion Peptide (pHLIP).Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Using Simulation to Understand the Role of Titration on the Stability of a Peptide-Lipid Bilayer Complex.Langmuir : the ACS journal of surfaces and colloids · 2020Article
- Kinetics of pHLIP peptide insertion into and exit from a membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Tumor-Targeted, Cytoplasmic Delivery of Large, Polar Molecules Using a pH-Low Insertion Peptide.Molecular pharmaceutics · 2020Article
- Targeting Acidic Diseased Tissues by pH-Triggered Membrane-Associated Peptide Folding.Frontiers in bioengineering and biotechnology · 2020Review
- Activity and characterization of a pH-sensitive antimicrobial peptide.Biochimica et biophysica acta. Biomembranes · 2019Article
- Ions Modulate Key Interactions between pHLIP and Lipid Membranes.Biophysical journal · 2019Article
- Cancer targeting peptides.Cellular and molecular life sciences : CMLS · 2019Review
- Phosphatidylserine Asymmetry Promotes the Membrane Insertion of a Transmembrane Helix.Biophysical journal · 2019Article
- Cooperative Nonbonded Forces Control Membrane Binding of the pH-Low Insertion Peptide pHLIP.Biophysical journal · 2018Article
- pH-dependent thermodynamic intermediates of pHLIP membrane insertion determined by solid-state NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Cooperativity Principles in Self-Assembled Nanomedicine.Chemical reviews · 2018Review
- Membrane-Induced p KJournal of chemical theory and computation · 2018Article
- Bilayer Thickness and Curvature Influence Binding and Insertion of a pHLIP Peptide.Biophysical journal · 2018Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The membrane-associated folding/unfolding of pH (low) insertion peptide (pHLIP) provides an opportunity to study how sequence variations influence the kinetics and pathway of peptide insertion into bilayers. Here, we present the results of steady-state and kinetics investigations of several pHLIP variants with different numbers of charged residues, with attached polar cargoes at the peptide's membrane-inserting end, and with three single-Trp variants placed at the beginning, middle, and end of the transmembrane helix. Each pHLIP variant exhibits a pH-dependent interaction with a lipid bilayer. Although the number of protonatable residues at the inserting end does not affect the ultimate formation of helical structure across a membrane, it correlates with the time for peptide insertion, the number of intermediate states on the folding pathway, and the rates of unfolding and exit. The presence of polar cargoes at the peptide's inserting end leads to the appearance of intermediate states on the insertion pathway. Cargo polarity correlates with a decrease of the insertion rate. We conclude that the existence of intermediate states on the folding and unfolding pathways is not mandatory and, in the simple case of a polypeptide with a noncharged and nonpolar inserting end, the folding and unfolding appears as an all-or-none transition. We propose a model for membrane-associated insertion/folding and exit/unfolding and discuss the importance of these observations for the design of new delivery agents for direct translocation of polar therapeutic and diagnostic cargo molecules across cellular membranes.
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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.