View in EDS

Surface-driven first-step events of nanoscale self-assembly for molecular peptide fibers: An experimental and theoretical study.

Saved in:
Bibliographic Details
Title: Surface-driven first-step events of nanoscale self-assembly for molecular peptide fibers: An experimental and theoretical study.
Authors: Forte, G.1, Messina, G.M.L.2, Zamuner, A.3, Dettin, M.3, Grassi, A.1, Marletta, G.2 gmarletta@unict.it
Source: Colloids & Surfaces B: Biointerfaces. Aug2018, Vol. 168, p148-155. 8p.
Subjects: Peptide analysis, Molecular dynamics, Electrostatic interaction, Surface interactions, Charge exchange
Abstract: New experimental results are reported on the self-assembling behavior of EAK16-II, the first discovered ionic self-complementary peptide, incubated at ultralow concentration (10 −6  M) at neutral pH onto differently charged surfaces. It is found that strongly negatively charged surfaces promote the self-assembly of flat, micrometer-long mono-molecular fibers of side-on assembled sequences, lying onto a continuous monolayer of flat-on EAK16-II molecules. These results suggest that the monomolecular EAK16-II self-assembly is driven by the peculiar matching condition between peptide and surface electrostatic properties. Molecular Mechanics simulations of the basic bimolecular interactions confirmed the experimental inferences, showing that the flat-on state is the most stable arrangement for two interacting EAK16-II sequences onto strongly negatively charged surfaces, where indeed EAK16-II β-sheet conformation is stabilized, while the weak electrostatic interactions with mildly charged substrates promote an “entangled” EAK16-II geometry. Molecular Dynamics simulations further showed that the mobility and diffusional freedom of the peptides from the surfaces are ruled by the relative strength of peptide-surface electrostatic interactions, so that desorption probability for the peptide sequences is negligible from strongly-charged surfaces and high from mildly-charged surfaces. Furthermore, it has been found that an oligopeptide sequence lying onto two flat-on EAK16-II molecules, gains a remarkable lateral mobility, while remaining weakly bound to the surface, thus allowing the further molecular self-alignment responsible for the micrometer-long fiber formation. The reported results pave the way to the understanding and control of the subtle peptide-surface structural motifs matching enabling the formation of micrometer-long, but nanometer-wide monomolecular fibers. [ABSTRACT FROM AUTHOR]
Copyright of Colloids & Surfaces B: Biointerfaces is the property of Elsevier B.V. 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: 129907823
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Surface-driven first-step events of nanoscale self-assembly for molecular peptide fibers: An experimental and theoretical study.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Forte%2C+G%2E%22">Forte, G.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Messina%2C+G%2EM%2EL%2E%22">Messina, G.M.L.</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Zamuner%2C+A%2E%22">Zamuner, A.</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Dettin%2C+M%2E%22">Dettin, M.</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Grassi%2C+A%2E%22">Grassi, A.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Marletta%2C+G%2E%22">Marletta, G.</searchLink><relatesTo>2</relatesTo><i> gmarletta@unict.it</i>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Colloids+%26+Surfaces+B%3A+Biointerfaces%22">Colloids & Surfaces B: Biointerfaces</searchLink>. Aug2018, Vol. 168, p148-155. 8p.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Peptide+analysis%22">Peptide analysis</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+dynamics%22">Molecular dynamics</searchLink><br /><searchLink fieldCode="DE" term="%22Electrostatic+interaction%22">Electrostatic interaction</searchLink><br /><searchLink fieldCode="DE" term="%22Surface+interactions%22">Surface interactions</searchLink><br /><searchLink fieldCode="DE" term="%22Charge+exchange%22">Charge exchange</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: New experimental results are reported on the self-assembling behavior of EAK16-II, the first discovered ionic self-complementary peptide, incubated at ultralow concentration (10 −6  M) at neutral pH onto differently charged surfaces. It is found that strongly negatively charged surfaces promote the self-assembly of flat, micrometer-long mono-molecular fibers of side-on assembled sequences, lying onto a continuous monolayer of flat-on EAK16-II molecules. These results suggest that the monomolecular EAK16-II self-assembly is driven by the peculiar matching condition between peptide and surface electrostatic properties. Molecular Mechanics simulations of the basic bimolecular interactions confirmed the experimental inferences, showing that the flat-on state is the most stable arrangement for two interacting EAK16-II sequences onto strongly negatively charged surfaces, where indeed EAK16-II β-sheet conformation is stabilized, while the weak electrostatic interactions with mildly charged substrates promote an “entangled” EAK16-II geometry. Molecular Dynamics simulations further showed that the mobility and diffusional freedom of the peptides from the surfaces are ruled by the relative strength of peptide-surface electrostatic interactions, so that desorption probability for the peptide sequences is negligible from strongly-charged surfaces and high from mildly-charged surfaces. Furthermore, it has been found that an oligopeptide sequence lying onto two flat-on EAK16-II molecules, gains a remarkable lateral mobility, while remaining weakly bound to the surface, thus allowing the further molecular self-alignment responsible for the micrometer-long fiber formation. The reported results pave the way to the understanding and control of the subtle peptide-surface structural motifs matching enabling the formation of micrometer-long, but nanometer-wide monomolecular fibers. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Colloids & Surfaces B: Biointerfaces is the property of Elsevier B.V. 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=129907823
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1016/j.colsurfb.2018.01.016
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 8
        StartPage: 148
    Subjects:
      – SubjectFull: Peptide analysis
        Type: general
      – SubjectFull: Molecular dynamics
        Type: general
      – SubjectFull: Electrostatic interaction
        Type: general
      – SubjectFull: Surface interactions
        Type: general
      – SubjectFull: Charge exchange
        Type: general
    Titles:
      – TitleFull: Surface-driven first-step events of nanoscale self-assembly for molecular peptide fibers: An experimental and theoretical study.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Forte, G.
      – PersonEntity:
          Name:
            NameFull: Messina, G.M.L.
      – PersonEntity:
          Name:
            NameFull: Zamuner, A.
      – PersonEntity:
          Name:
            NameFull: Dettin, M.
      – PersonEntity:
          Name:
            NameFull: Grassi, A.
      – PersonEntity:
          Name:
            NameFull: Marletta, G.
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 08
              Text: Aug2018
              Type: published
              Y: 2018
          Identifiers:
            – Type: issn-print
              Value: 09277765
          Numbering:
            – Type: volume
              Value: 168
          Titles:
            – TitleFull: Colloids & Surfaces B: Biointerfaces
              Type: main
ResultId 1