Exploring the Impact of Subtle Differences in the Chemical Structure of 1-Alkylsulfates and 1-Alkylsulfonates on Their Interactions with Human Serum Albumin.

Ola Grabowska, Ankur Singh, Krzysztof Żamojć, Sergey A Samsonov, Dariusz Wyrzykowski

Abstract read

In one paragraph

Article in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact

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

1 citing paper in PubMed.

Cyclodextrin and KR12-Lipopeptide Interactions: A Thermodynamic View of Binding Mechanisms and Impact on the Structure of α-Helical Peptides.The journal of physical chemistry. B · 2026
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.

Ola GrabowskaFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, Poland.

Ankur SinghFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, Poland.

Krzysztof ŻamojćFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, Poland.ORCID 0000-0002-4756-1927

Sergey A SamsonovFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, Poland.ORCID 0000-0002-5166-4849

Dariusz WyrzykowskiFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, Poland.ORCID 0000-0002-3823-3286

Funding

National Science Center UMO-2023/49/B/ST4/00041The grants for Young Scientists 2023 from University of Gdansk, Poland 539-T090-B989-23

6 · The paper itself

Abstract

The objective of this study was to examine the interactions between anionic surfactants, specifically 1-alkylsulfonates (KXS) and 1-alkylsulfates (SXS) ions, with human serum albumin (HSA). A combination of experimental techniques, including isothermal titration calorimetry (ITC), steady-state fluorescence spectroscopy (SF), and molecular dynamics-based approaches was employed to gain a comprehensive understanding of these processes. It has been demonstrated that the subtle variations in the charge distribution on the anionic surfactant headgroups have a significant impact on the number of binding sites, the stoichiometry of the resulting complexes, and the strength of the interactions between the surfactants and the protein. Additionally, we established that the affinity of the investigated ligands to specific regions on the protein surface is governed by both the charge of the surfactant headgroup and the length of the aliphatic hydrocarbon chain. In summary, the findings highlight the crucial role of charge distribution on surfactant functional groups in the binding mode and the thermodynamic stability of surfactant-protein complexes.

Indexed as

Protein BindingSerum Albumin, HumanSurface-Active AgentsThermodynamicsAlkanesulfonatesBinding SitesCalorimetryHumansMolecular Dynamics SimulationMolecular StructureSpectrometry, FluorescenceAlkanesulfonatesSerum Albumin, HumanSurface-Active Agents1-alkylsulfates1-alkylsulfonatesfluorescence spectroscopyhuman serum albuminisothermal titration calorimetrymolecular dynamicsprotein–ligand interactions

Identifiers

PMID39407528

DOI10.3390/molecules29194598

PMCPMC11478022

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.