Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres

Ricardo M.P. Da Silva; Daan Van Der Zwaag; Lorenzo Albertazzi; Sungsoo S. Lee; E. W. Meijer; Samuel I. Stupp

doi:10.1038/ncomms11561

Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres

Ricardo M.P. Da Silva, Daan Van Der Zwaag, Lorenzo Albertazzi, Sungsoo S. Lee, E. W. Meijer, Samuel I. Stupp

Northwestern University

Research output: Contribution to journal › Article › peer-review

71 Citations (Scopus)

Abstract

The dynamic behaviour of supramolecular systems is an important dimension of their potential functions. Here, we report on the use of stochastic optical reconstruction microscopy to study the molecular exchange of peptide amphiphile nanofibres, supramolecular systems known to have important biomedical functions. Solutions of nanofibres labelled with different dyes (Cy3 and Cy5) were mixed, and the distribution of dyes inserting into initially single-colour nanofibres was quantified using correlative image analysis. Our observations are consistent with an exchange mechanism involving monomers or small clusters of molecules inserting randomly into a fibre. Different exchange rates are observed within the same fibre, suggesting that local cohesive structures exist on the basis of β-sheet discontinuous domains. The results reported here show that peptide amphiphile supramolecular systems can be dynamic and that their intermolecular interactions affect exchange patterns. This information can be used to generate useful aggregate morphologies for improved biomedical function.

Original language	English
Article number	11561
Journal	Nature communications
Volume	7
DOIs	https://doi.org/10.1038/ncomms11561
Publication status	Published - May 19 2016

ASJC Scopus subject areas

Chemistry(all)
Biochemistry, Genetics and Molecular Biology(all)
Physics and Astronomy(all)

Access to Document

10.1038/ncomms11561

Fingerprint Dive into the research topics of 'Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres'. Together they form a unique fingerprint.

Cite this

@article{a1211101e1c64bc6a6ea435df3d36814,

title = "Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres",

abstract = "The dynamic behaviour of supramolecular systems is an important dimension of their potential functions. Here, we report on the use of stochastic optical reconstruction microscopy to study the molecular exchange of peptide amphiphile nanofibres, supramolecular systems known to have important biomedical functions. Solutions of nanofibres labelled with different dyes (Cy3 and Cy5) were mixed, and the distribution of dyes inserting into initially single-colour nanofibres was quantified using correlative image analysis. Our observations are consistent with an exchange mechanism involving monomers or small clusters of molecules inserting randomly into a fibre. Different exchange rates are observed within the same fibre, suggesting that local cohesive structures exist on the basis of β-sheet discontinuous domains. The results reported here show that peptide amphiphile supramolecular systems can be dynamic and that their intermolecular interactions affect exchange patterns. This information can be used to generate useful aggregate morphologies for improved biomedical function.",

author = "{Da Silva}, {Ricardo M.P.} and {Van Der Zwaag}, Daan and Lorenzo Albertazzi and Lee, {Sungsoo S.} and Meijer, {E. W.} and Stupp, {Samuel I.}",

note = "Funding Information: Molecular synthesis, purification and characterization were supported by the U.S. Department of Energy, Office of Science, Basic Energy Sciences, under Award # DE-FG02-00ER45810. The work in Eindhoven was supported by was financed by the Dutch Ministry of Education, Culture and Science (Gravity program 024.001.035) and the European Research Council (FP7/2007-2013, ERC Grant Agreement 246829). R.M.P.d.S. and his research activities were funded by the Marie Curie FP7-PEOPLE-2010-IOF program (ref. no. 273295). Compound preparation, purification and characterization were partially performed at the Peptide Synthesis Core at Simpson Querrey Institute. The Biological Imaging Facility (BIF) and Keck Biophysics facilities at Northwestern provided further instrumentation used in this work. Mark Seniw is acknowledged for the preparation of graphics.",

year = "2016",

month = may,

day = "19",

doi = "10.1038/ncomms11561",

language = "English",

volume = "7",

journal = "Nature Communications",

issn = "2041-1723",

publisher = "Nature Publishing Group",

}

TY - JOUR

T1 - Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres

AU - Da Silva, Ricardo M.P.

AU - Van Der Zwaag, Daan

AU - Albertazzi, Lorenzo

AU - Lee, Sungsoo S.

AU - Meijer, E. W.

AU - Stupp, Samuel I.

N1 - Funding Information: Molecular synthesis, purification and characterization were supported by the U.S. Department of Energy, Office of Science, Basic Energy Sciences, under Award # DE-FG02-00ER45810. The work in Eindhoven was supported by was financed by the Dutch Ministry of Education, Culture and Science (Gravity program 024.001.035) and the European Research Council (FP7/2007-2013, ERC Grant Agreement 246829). R.M.P.d.S. and his research activities were funded by the Marie Curie FP7-PEOPLE-2010-IOF program (ref. no. 273295). Compound preparation, purification and characterization were partially performed at the Peptide Synthesis Core at Simpson Querrey Institute. The Biological Imaging Facility (BIF) and Keck Biophysics facilities at Northwestern provided further instrumentation used in this work. Mark Seniw is acknowledged for the preparation of graphics.

PY - 2016/5/19

Y1 - 2016/5/19

N2 - The dynamic behaviour of supramolecular systems is an important dimension of their potential functions. Here, we report on the use of stochastic optical reconstruction microscopy to study the molecular exchange of peptide amphiphile nanofibres, supramolecular systems known to have important biomedical functions. Solutions of nanofibres labelled with different dyes (Cy3 and Cy5) were mixed, and the distribution of dyes inserting into initially single-colour nanofibres was quantified using correlative image analysis. Our observations are consistent with an exchange mechanism involving monomers or small clusters of molecules inserting randomly into a fibre. Different exchange rates are observed within the same fibre, suggesting that local cohesive structures exist on the basis of β-sheet discontinuous domains. The results reported here show that peptide amphiphile supramolecular systems can be dynamic and that their intermolecular interactions affect exchange patterns. This information can be used to generate useful aggregate morphologies for improved biomedical function.

AB - The dynamic behaviour of supramolecular systems is an important dimension of their potential functions. Here, we report on the use of stochastic optical reconstruction microscopy to study the molecular exchange of peptide amphiphile nanofibres, supramolecular systems known to have important biomedical functions. Solutions of nanofibres labelled with different dyes (Cy3 and Cy5) were mixed, and the distribution of dyes inserting into initially single-colour nanofibres was quantified using correlative image analysis. Our observations are consistent with an exchange mechanism involving monomers or small clusters of molecules inserting randomly into a fibre. Different exchange rates are observed within the same fibre, suggesting that local cohesive structures exist on the basis of β-sheet discontinuous domains. The results reported here show that peptide amphiphile supramolecular systems can be dynamic and that their intermolecular interactions affect exchange patterns. This information can be used to generate useful aggregate morphologies for improved biomedical function.

UR - http://www.scopus.com/inward/record.url?scp=84970022034&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84970022034&partnerID=8YFLogxK

U2 - 10.1038/ncomms11561

DO - 10.1038/ncomms11561

M3 - Article

C2 - 27194204

AN - SCOPUS:84970022034

VL - 7

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 11561

ER -