View in EDS

Adsorption of proteins to fluid interfaces: Role of the hydrophobic subphase.

Saved in:
Bibliographic Details
Title: Adsorption of proteins to fluid interfaces: Role of the hydrophobic subphase.
Authors: Bergfreund, Jotam1 (AUTHOR) jotam.bergfreund@hest.ethz.ch, Bertsch, Pascal1 (AUTHOR), Fischer, Peter1 (AUTHOR) peter.fischer@hest.ethz.ch
Source: Journal of Colloid & Interface Science. Feb2021, Vol. 584, p411-417. 7p.
Subjects: Hydrophobic interactions, Protein-protein interactions, Globular proteins, Cytoskeletal proteins, Denaturation of proteins, Adsorption (Chemistry), Proteins
Abstract: Adsorption of proteins to fluid interfaces is critical in many industries, scientific disciplines, and biological processes. However, the structural transitions of proteins upon adsorption and the effect of the hydrophobic subphase, such as oil, have received little attention. Herein, we present a comprehensive study on the effect of the hydrophobic subphase on the adsorption behavior of globular and random-coil proteins. The adsorption of proteins is limited by their structural stability, and accordingly, is faster for less stable globular proteins and fastest for random-coil proteins. Protein adsorption is slower at more polar oils, regardless of the protein type, structure, and stability. Moreover, we found a correlation of oil polarity and the induced surface pressure of proteins, which seems universally applicable and describes the experimental data of over 30 previous studies. The model works for all commonly applied subphases, with the exception of oils that chemically react with proteins (e.g. octanal) and air, due to the lack of hydrophobic interactions. These results foster our understanding of protein adsorption and allow the prediction of protein unfolding depending on protein-subphase interactions. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Colloid & Interface Science is the property of Academic Press Inc. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
FullText Text:
  Availability: 0
Header DbId: egs
DbLabel: Engineering Source
An: 147522011
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Adsorption of proteins to fluid interfaces: Role of the hydrophobic subphase.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Bergfreund%2C+Jotam%22">Bergfreund, Jotam</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> jotam.bergfreund@hest.ethz.ch</i><br /><searchLink fieldCode="AR" term="%22Bertsch%2C+Pascal%22">Bertsch, Pascal</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Fischer%2C+Peter%22">Fischer, Peter</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> peter.fischer@hest.ethz.ch</i>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Journal+of+Colloid+%26+Interface+Science%22">Journal of Colloid & Interface Science</searchLink>. Feb2021, Vol. 584, p411-417. 7p.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Hydrophobic+interactions%22">Hydrophobic interactions</searchLink><br /><searchLink fieldCode="DE" term="%22Protein-protein+interactions%22">Protein-protein interactions</searchLink><br /><searchLink fieldCode="DE" term="%22Globular+proteins%22">Globular proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Cytoskeletal+proteins%22">Cytoskeletal proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Denaturation+of+proteins%22">Denaturation of proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Adsorption+%28Chemistry%29%22">Adsorption (Chemistry)</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Adsorption of proteins to fluid interfaces is critical in many industries, scientific disciplines, and biological processes. However, the structural transitions of proteins upon adsorption and the effect of the hydrophobic subphase, such as oil, have received little attention. Herein, we present a comprehensive study on the effect of the hydrophobic subphase on the adsorption behavior of globular and random-coil proteins. The adsorption of proteins is limited by their structural stability, and accordingly, is faster for less stable globular proteins and fastest for random-coil proteins. Protein adsorption is slower at more polar oils, regardless of the protein type, structure, and stability. Moreover, we found a correlation of oil polarity and the induced surface pressure of proteins, which seems universally applicable and describes the experimental data of over 30 previous studies. The model works for all commonly applied subphases, with the exception of oils that chemically react with proteins (e.g. octanal) and air, due to the lack of hydrophobic interactions. These results foster our understanding of protein adsorption and allow the prediction of protein unfolding depending on protein-subphase interactions. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Colloid & Interface Science is the property of Academic Press Inc. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=147522011
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1016/j.jcis.2020.09.118
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 7
        StartPage: 411
    Subjects:
      – SubjectFull: Hydrophobic interactions
        Type: general
      – SubjectFull: Protein-protein interactions
        Type: general
      – SubjectFull: Globular proteins
        Type: general
      – SubjectFull: Cytoskeletal proteins
        Type: general
      – SubjectFull: Denaturation of proteins
        Type: general
      – SubjectFull: Adsorption (Chemistry)
        Type: general
      – SubjectFull: Proteins
        Type: general
    Titles:
      – TitleFull: Adsorption of proteins to fluid interfaces: Role of the hydrophobic subphase.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Bergfreund, Jotam
      – PersonEntity:
          Name:
            NameFull: Bertsch, Pascal
      – PersonEntity:
          Name:
            NameFull: Fischer, Peter
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 15
              M: 02
              Text: Feb2021
              Type: published
              Y: 2021
          Identifiers:
            – Type: issn-print
              Value: 00219797
          Numbering:
            – Type: volume
              Value: 584
          Titles:
            – TitleFull: Journal of Colloid & Interface Science
              Type: main
ResultId 1