ArticleACS omega2017
Protonation Enhances the Inherent Helix-Forming Propensity of pHLIP.
Article in ACS omega, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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.
Who cites it
11 citing papers in PubMed.
- Small animal PET imaging with theEJNMMI radiopharmacy and chemistry · 2024Article
- Arginine Residues Modulate the Membrane Interactions of pHLIP Peptides.Journal of chemical information and modeling · 2023Article
- Recent Advances in Imaging Agents Anchored with pH (Low) Insertion Peptides for Cancer Theranostics.Molecules (Basel, Switzerland) · 2023Review
- Peptide-Based Drug Delivery Systems.Medicina (Kaunas, Lithuania) · 2021Review
- Guardians of the Cell: State-of-the-Art of Membrane Proteins from a Computational Point-of-View.Methods in molecular biology (Clifton, N.J.) · 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
- 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
- Cooperative Nonbonded Forces Control Membrane Binding of the pH-Low Insertion Peptide pHLIP.Biophysical journal · 2018Article
- Membrane-Induced p KJournal of chemical theory and computation · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Cell-penetrating peptides (CPPs) can be potentially used in targeted delivery of therapeutic cargoes. However, their conformation in solution is poorly understood. We employed molecular dynamics simulations to probe the structural fluctuations of an anionic CPP, pH Low Insertion Peptide (pHLIP), in solution to determine the effects of modifications to selected residues on the structure of pHLIP. Two types of modifications were tested: (1) protonation of aspartic acid residues and (2) point mutations known to affect the acid sensitivity of pHLIP. pHLIP samples conformations ranging from coil to helix to sheet, and modifications to pHLIP lead to subtle shifts in the balance between these conformations. In some instances, pHLIP is as likely to form a helical conformation as it is to form an unstructured coil. Understanding the behavior of pHLIP in solution is necessary for determining optimal conditions for administration of pHLIP and design of promising pHLIP variants.
Identifiers
What OpenQuestion holds
Registered trials
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.