Evidence map›Paper›PMID 18829441›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Energetics of peptide (pHLIP) binding to and folding across a lipid bilayer membrane.

Yana K Reshetnyak, Oleg A Andreev, Michael Segala, Vladislav S Markin, Donald M Engelman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
2.8field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

101 citing papers in PubMed, 191 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Small animal PET imaging with theEJNMMI radiopharmacy and chemistry · 2024
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. pHLIP Peptides Target Acidity in Activated Macrophages.Molecular imaging and biology · 2022
    Article
  16. CaProtein science : a publication of the Protein Society · 2022
    Article
  17. Review
  18. Article
  19. Cancer heterogeneity and metastasis: life at the edge.Clinical & experimental metastasis · 2022
    Review
  20. Article

41 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Yana K ReshetnyakPhysics Department, University of Rhode Island, 2 Lippitt Road, Kingston, RI 02881, USA. reshetnyak@mail.uri.edu
Oleg A Andreev
Michael Segala
Vladislav S Markin
Donald M Engelman
University of Rhode Island · USThe University of Texas Southwestern Medical Center · USYale University · US

Funding

TM INTERACTIONS IN MEMBRANE PROTEIN FOLDING AND FUNCTIONR01GM073857 · NIGMS · YALE UNIVERSITY · PI ANDREEV, OLEG A, ENGELMAN, DONALD M. · 2006 to 2023
$8.4M
MOLECULAR FACTORS IN BIOMEMBRANE THICKNESSESR01GM070895 · NIGMS · YALE UNIVERSITY · PI ENGELMAN, DONALD M · 2004 to 2007
$1.2M
New Technology for Selective Delivery of PNAs in Cancer Cells In Vitro and In VivR21CA125280 · NCI · UNIVERSITY OF RHODE ISLAND · PI ANDREEV, OLEG A · 2007 to 2008
$278k
NCI NIH HHS R21 CA125280NIGMS NIH HHS GM070895NIGMS NIH HHS GM073857NIGMS NIH HHS R01 GM070895NIGMS NIH HHS R01 GM073857PHS HHS RCA125280A
6 · The paper itself

Abstract

The pH low-insertion peptide (pHLIP) serves as a model system for peptide insertion and folding across a lipid bilayer. It has three general states: (I) soluble in water or (II) bound to the surface of a lipid bilayer as an unstructured monomer, and (III) inserted across the bilayer as a monomeric alpha-helix. We used fluorescence spectroscopy and isothermal titration calorimetry to study the interactions of pHLIP with a palmitoyloleoylphosphatidylcholine (POPC) lipid bilayer and to calculate the transition energies between states. We found that the Gibbs free energy of binding to a POPC surface at low pHLIP concentration (state I-state II transition) at 37 degrees C is approximately -7 kcal/mol near neutral pH and that the free energy of insertion and folding across a lipid bilayer at low pH (state II-state III transition) is nearly -2 kcal/mol. We discuss a number of related thermodynamic parameters from our measurements. Besides its fundamental interest as a model system for the study of membrane protein folding, pHLIP has utility as an agent to target diseased tissues and translocate molecules through the membrane into the cytoplasm of cells in environments with elevated levels of extracellular acidity, as in cancer and inflammation. The results give the amount of energy that might be used to move cargo molecules across a membrane.

Indexed as

Base SequenceBinding SitesHydrogen-Ion ConcentrationKineticsLipid BilayersMembrane FluidityMembrane ProteinsModels, BiologicalMolecular Sequence DataPeptidesProtein FoldingSpectrometry, FluorescenceThermodynamicsLipid BilayersMembrane ProteinsPeptidespHLIP protein

Identifiers

PMID18829441
PMCPMC2556629
OpenAlexW2065100627

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.