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Analysis of institutional authors

Samhan-Arias, Alejandro KCorresponding Author

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January 2, 2023
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Biochemical and Biophysical Characterization of the Caveolin-2 Interaction with Membranes and Analysis of the Protein Structural Alteration by the Presence of Cholesterol

Publicated to:INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. 23 (23): 15203- - 2022-12-01 23(23), DOI: 10.3390/ijms232315203

Authors: Gorospe, Berta; Moura, Jose J. G.; Gutierrez-Merino, Carlos; Samhan-Arias, Alejandro K.;

Affiliations

Inst Invest Biomed Alberto Sols CS UAM, C Arturo Duperier 4, Madrid 28029, Spain - Author
Univ Autonoma Madrid UAM, Dept Bioquim, C Arturo Duperier 4, Madrid 28029, Spain - Author
Univ Extremadura, Res Inst Mol Pathol Biomarkers, Badajoz 06006, Spain - Author
Univ Nova Lisboa, Fac Ciencias & Tecnol, Dept Quim, LAQV REQUIMTE, P-2829516 Lisbon, Portugal - Author

Abstract

Caveolin-2 is a protein suitable for the study of interactions of caveolins with other proteins and lipids present in caveolar lipid rafts. Caveolin-2 has a lower tendency to associate with high molecular weight oligomers than caveolin-1, facilitating the study of its structural modulation upon association with other proteins or lipids. In this paper, we have successfully expressed and purified recombinant human caveolin-2 using E. coli. The structural changes of caveolin-2 upon interaction with a lipid bilayer of liposomes were characterized using bioinformatic prediction models, circular dichroism, differential scanning calorimetry, and fluorescence techniques. Our data support that caveolin-2 binds and alters cholesterol-rich domains in the membranes through a CARC domain, a type of cholesterol-interacting domain in its sequence. The far UV-CD spectra support that the purified protein keeps its folding properties but undergoes a change in its secondary structure in the presence of lipids that correlates with the acquisition of a more stable conformation, as shown by differential scanning calorimetry experiments. Fluorescence experiments using egg yolk lecithin large unilamellar vesicles loaded with 1,6-diphenylhexatriene confirmed that caveolin-2 adsorbs to the membrane but only penetrates the core of the phospholipid bilayer if vesicles are supplemented with 30% of cholesterol. Our study sheds light on the caveolin-2 interaction with lipids. In addition, we propose that purified recombinant caveolin-2 can provide a new tool to study protein-lipid interactions within caveolae.

Keywords

caveolin-1caveolin-2cholesterolmembrane interactionC-terminal domainCaveolin-1Caveolin-2CholesterolCytochrome b(5) reductaseExpressionIdentificationMembrane interactionMultiple sequence alignmentMutational analysisNitric-oxidePlasma-membraneScaffolding domainSecondary structure predictionSuperoxide anion

Quality index

Bibliometric impact. Analysis of the contribution and dissemination channel

The work has been published in the journal INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES due to its progression and the good impact it has achieved in recent years, according to the agency WoS (JCR), it has become a reference in its field. In the year of publication of the work, 2022, it was in position 66/285, thus managing to position itself as a Q1 (Primer Cuartil), in the category Biochemistry & Molecular Biology.

Independientemente del impacto esperado determinado por el canal de difusión, es importante destacar el impacto real observado de la propia aportación.

Según las diferentes agencias de indexación, el número de citas acumuladas por esta publicación hasta la fecha 2025-07-18:

  • WoS: 1
  • Scopus: 1
  • Europe PMC: 1

Impact and social visibility

From the perspective of influence or social adoption, and based on metrics associated with mentions and interactions provided by agencies specializing in calculating the so-called "Alternative or Social Metrics," we can highlight as of 2025-07-18:

  • The use of this contribution in bookmarks, code forks, additions to favorite lists for recurrent reading, as well as general views, indicates that someone is using the publication as a basis for their current work. This may be a notable indicator of future more formal and academic citations. This claim is supported by the result of the "Capture" indicator, which yields a total of: 7 (PlumX).

It is essential to present evidence supporting full alignment with institutional principles and guidelines on Open Science and the Conservation and Dissemination of Intellectual Heritage. A clear example of this is:

  • The work has been submitted to a journal whose editorial policy allows open Open Access publication.
  • Assignment of a Handle/URN as an identifier within the deposit in the Institutional Repository: https://repositorio.uam.es/handle/10486/711203

Leadership analysis of institutional authors

This work has been carried out with international collaboration, specifically with researchers from: Portugal.

There is a significant leadership presence as some of the institution’s authors appear as the first or last signer, detailed as follows: Last Author (SAMHAN ARIAS, ALEJANDRO KHALIL).

the author responsible for correspondence tasks has been SAMHAN ARIAS, ALEJANDRO KHALIL.