IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v15y2024i1d10.1038_s41467-024-53966-z.html
   My bibliography  Save this article

Small molecule modulation of protein corona for deep plasma proteome profiling

Author

Listed:
  • Ali Akbar Ashkarran

    (Michigan State University
    Michigan State University)

  • Hassan Gharibi

    (Karolinska Institutet)

  • Seyed Amirhossein Sadeghi

    (Michigan State University)

  • Seyed Majed Modaresi

    (University of Basel)

  • Qianyi Wang

    (Michigan State University)

  • Teng-Jui Lin

    (University of California, Berkeley)

  • Ghafar Yerima

    (University of California Berkeley)

  • Ali Tamadon

    (University of California Berkeley)

  • Maryam Sayadi

    (Michigan State University)

  • Maryam Jafari

    (Karolinska Institutet)

  • Zijin Lin

    (Michigan State University)

  • Danilo Ritz

    (University of Basel)

  • David Kakhniashvili

    (University of Tennessee Health Science Center)

  • Avirup Guha

    (Medical College of Georgia at Augusta University)

  • Mohammad R. K. Mofrad

    (University of California Berkeley)

  • Liangliang Sun

    (Michigan State University)

  • Markita P. Landry

    (University of California, Berkeley
    Berkeley
    Chan Zuckerberg Biohub)

  • Amir Ata Saei

    (Karolinska Institutet)

  • Morteza Mahmoudi

    (Michigan State University
    Michigan State University)

Abstract

The protein corona formed on nanoparticles (NPs) has potential as a valuable diagnostic tool for improving plasma proteome coverage. Here, we show that spiking small molecules, including metabolites, lipids, vitamins, and nutrients into plasma can induce diverse protein corona patterns on otherwise identical NPs, significantly enhancing the depth of plasma proteome profiling. The protein coronas on polystyrene NPs when exposed to plasma treated with an array of small molecules allows for the detection of 1793 proteins marking an 8.25-fold increase in the number of quantified proteins compared to plasma alone (218 proteins) and a 2.63-fold increase relative to the untreated protein corona (681 proteins). Furthermore, we discovered that adding 1000 µg/ml phosphatidylcholine could singularly enable the detection of 897 proteins. At this specific concentration, phosphatidylcholine selectively depletes the four most abundant plasma proteins, including albumin, thus reducing the dynamic range of plasma proteome and enabling the detection of proteins with lower abundance. Employing an optimized data-independent acquisition approach, the inclusion of phosphatidylcholine leads to the detection of 1436 proteins in a single plasma sample. Our molecular dynamics results reveal that phosphatidylcholine interacts with albumin via hydrophobic interactions, H-bonds, and water bridges. The addition of phosphatidylcholine also enables the detection of 337 additional proteoforms compared to untreated protein corona using a top-down proteomics approach. Given the critical role of plasma proteomics in biomarker discovery and disease monitoring, we anticipate the widespread adoption of this methodology for the identification and clinical translation of biomarkers.

Suggested Citation

  • Ali Akbar Ashkarran & Hassan Gharibi & Seyed Amirhossein Sadeghi & Seyed Majed Modaresi & Qianyi Wang & Teng-Jui Lin & Ghafar Yerima & Ali Tamadon & Maryam Sayadi & Maryam Jafari & Zijin Lin & Danilo , 2024. "Small molecule modulation of protein corona for deep plasma proteome profiling," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
  • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-53966-z
    DOI: 10.1038/s41467-024-53966-z
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-024-53966-z
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-024-53966-z?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Morteza Mahmoudi, 2022. "The need for improved methodology in protein corona analysis," Nature Communications, Nature, vol. 13(1), pages 1-4, December.
    2. Hassan Gharibi & Ali Akbar Ashkarran & Maryam Jafari & Elizabeth Voke & Markita P. Landry & Amir Ata Saei & Morteza Mahmoudi, 2024. "A uniform data processing pipeline enables harmonized nanoparticle protein corona analysis across proteomics core facilities," Nature Communications, Nature, vol. 15(1), pages 1-9, December.
    3. Ali Akbar Ashkarran & Hassan Gharibi & Elizabeth Voke & Markita P. Landry & Amir Ata Saei & Morteza Mahmoudi, 2022. "Measurements of heterogeneity in proteomics analysis of the nanoparticle protein corona across core facilities," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    4. Sara Sheibani & Kaustuv Basu & Ali Farnudi & Aliakbar Ashkarran & Muneyoshi Ichikawa & John F. Presley & Khanh Huy Bui & Mohammad Reza Ejtehadi & Hojatollah Vali & Morteza Mahmoudi, 2021. "Nanoscale characterization of the biomolecular corona by cryo-electron microscopy, cryo-electron tomography, and image simulation," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
    5. Amir Ata Saei & Christian Michel Beusch & Alexey Chernobrovkin & Pierre Sabatier & Bo Zhang & Ülkü Güler Tokat & Eleni Stergiou & Massimiliano Gaetani & Ákos Végvári & Roman A. Zubarev, 2019. "ProTargetMiner as a proteome signature library of anticancer molecules for functional discovery," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Ali Akbar Ashkarran & Hassan Gharibi & Elizabeth Voke & Markita P. Landry & Amir Ata Saei & Morteza Mahmoudi, 2022. "Measurements of heterogeneity in proteomics analysis of the nanoparticle protein corona across core facilities," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Didar Baimanov & Jing Wang & Jun Zhang & Ke Liu & Yalin Cong & Xiaomeng Shi & Xiaohui Zhang & Yufeng Li & Xiumin Li & Rongrong Qiao & Yuliang Zhao & Yunlong Zhou & Liming Wang & Chunying Chen, 2022. "In situ analysis of nanoparticle soft corona and dynamic evolution," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. Hassan Gharibi & Ali Akbar Ashkarran & Maryam Jafari & Elizabeth Voke & Markita P. Landry & Amir Ata Saei & Morteza Mahmoudi, 2024. "A uniform data processing pipeline enables harmonized nanoparticle protein corona analysis across proteomics core facilities," Nature Communications, Nature, vol. 15(1), pages 1-9, December.
    4. Victoria O. Shender & Ksenia S. Anufrieva & Polina V. Shnaider & Georgij P. Arapidi & Marat S. Pavlyukov & Olga M. Ivanova & Irina K. Malyants & Grigory A. Stepanov & Evgenii Zhuravlev & Rustam H. Zig, 2024. "Therapy-induced secretion of spliceosomal components mediates pro-survival crosstalk between ovarian cancer cells," Nature Communications, Nature, vol. 15(1), pages 1-26, December.
    5. Pierre Sabatier & Christian M. Beusch & Amir A. Saei & Mike Aoun & Noah Moruzzi & Ana Coelho & Niels Leijten & Magnus Nordenskjöld & Patrick Micke & Diana Maltseva & Alexander G. Tonevitsky & Vincent , 2021. "An integrative proteomics method identifies a regulator of translation during stem cell maintenance and differentiation," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    6. Aleksandr Ianevski & Kristen Nader & Kyriaki Driva & Wojciech Senkowski & Daria Bulanova & Lidia Moyano-Galceran & Tanja Ruokoranta & Heikki Kuusanmäki & Nemo Ikonen & Philipp Sergeev & Markus Vähä-Ko, 2024. "Single-cell transcriptomes identify patient-tailored therapies for selective co-inhibition of cancer clones," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-53966-z. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.