Evidence map›Paper›PMID 36077155›Full record

ReviewInternational journal of molecular sciences2022

Analysis of the Equilibrium Distribution of Ligands in Heterogeneous Media-Approaches and Pitfalls.

Maria João Moreno, Luís M S Loura, Jorge Martins, Armindo Salvador, Adrian Velazquez-Campoy

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

7 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
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 4 institutions in 2 countries.

Maria João MorenoCoimbra Chemistry Center-Institute of Molecular Sciences (CQC-IMS), University of Coimbra, 3004-535 Coimbra, Portugal.ORCID 0000-0003-3076-9905
Luís M S LouraCoimbra Chemistry Center-Institute of Molecular Sciences (CQC-IMS), University of Coimbra, 3004-535 Coimbra, Portugal.ORCID 0000-0002-1051-2312
Jorge MartinsCentro de Ciências do Mar (CCMAR/CIMAR, LA) and DCBB-FCT, Universidade do Algarve, Campus de Gambelas, 8005-139 Faro, Portugal.ORCID 0000-0001-5460-1969
Armindo SalvadorCoimbra Chemistry Center-Institute of Molecular Sciences (CQC-IMS), University of Coimbra, 3004-535 Coimbra, Portugal.ORCID 0000-0002-4442-4900
Adrian Velazquez-CampoyInstitute for Biocomputation and Physics of Complex Systems (BIFI), Joint Unit GBsC-CSIC-BIFI, Universidad de Zaragoza, 50018 Zaragoza, Spain.ORCID 0000-0001-5702-4538
University of Coimbra · PTCentro de Neurociências e Biologia Celular · PTUniversidad de Zaragoza · ESUniversity of Algarve · PT

Funding

Fundação para a Ciência e Tecnologia UIDB/04539/2020, UIDP/04539/2020, UIDB/00313/2020, UIDP/00313/2020
6 · The paper itself

Abstract

The equilibrium distribution of small molecules (ligands) between binding agents in heterogeneous media is an important property that determines their activity. Heterogeneous systems containing proteins and lipid membranes are particularly relevant due to their prevalence in biological systems, and their importance to ligand distribution, which, in turn, is crucial to ligand's availability and biological activity. In this work, we review several approaches and formalisms for the analysis of the equilibrium distribution of ligands in the presence of proteins, lipid membranes, or both. Special attention is given to common pitfalls in the analysis, with the establishment of the validity limits for the distinct approaches. Due to its widespread use, special attention is given to the characterization of ligand binding through the analysis of Stern-Volmer plots of protein fluorescence quenching. Systems of increasing complexity are considered, from proteins with single to multiple binding sites, from ligands interacting with proteins only to biomembranes containing lipid bilayers and membrane proteins. A new formalism is proposed, in which ligand binding is treated as a partition process, while considering the saturation of protein binding sites. This formalism is particularly useful for the characterization of interaction with membrane proteins.

Indexed as

Lipid BilayersMembrane ProteinsBinding SitesLigandsProtein BindingLigandsLipid BilayersMembrane Proteinsbinding affinitybiomembraneslipid bilayerspartition coefficientproteinsScatchard plotsStern–Volmer plots

Identifiers

PMID36077155
PMCPMC9478965
OpenAlexW4293426339

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.