Amyloid-derived peptide forms self-assembled monolayers on gold nanoparticle with a curvature-dependent β-sheet structure

Chemistry

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https://doi.org/10.1021/nn204214x
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Keywords

Amino Acid Sequence, Amyloid, Gold, Hydrogen Bonding, Magnetic Resonance Spectroscopy, Metal Nanoparticles, Particle Size, Peptide Fragments, Protein Structure, Secondary, Spectroscopy, Fourier Transform Infrared, Water

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Amyloid-derived peptide forms self-assembled monolayers on gold nanoparticle with a curvature-dependent β-sheet structure. / Shaw, Christopher P; Middleton, David A; Volk, Martin et al.
In: ACS Nano, Vol. 6, No. 2, 28.02.2012, p. 1416-26.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Bibtex

@article{b5121f257b6044afa587c04488a201bb,

title = "Amyloid-derived peptide forms self-assembled monolayers on gold nanoparticle with a curvature-dependent β-sheet structure",

abstract = "Using a combination of Fourier transform infrared (FTIR) spectroscopy and solid-state nuclear magnetic resonance (SSNMR) techniques, the secondary structure of peptides anchored on gold nanoparticles of different sizes is investigated. The structure of the well-studied CALNN-capped nanoparticles is compared to the structure of nanoparticles capped with a new cysteine-terminated peptide, CFGAILSS. The design of that peptide is derived from the minimal amyloidogenic sequence FGAIL of the human islet polypeptide amylin. We demonstrate that CFGAILSS forms extended fibrils in solution. When constrained at a nanoparticle surface, CFGAILSS adopts a secondary structure markedly different from CALNN. Taking into account the surface selection rules, the FTIR spectra of CFGAILSS-capped gold nanoparticles indicate the formation of β-sheets which are more prominent for 25 nm diameter nanoparticles than for 5 nm nanoparticles. No intermolecular (13)C-(13)C dipolar coupling is detected with rotational resonance SSNMR for CALNN-capped nanoparticles, while CALNN is in a random coil configuration. Coupling is detected for CFGAILSS-capped gold nanoparticles, however, consistent with an intermolecular (13)C-(13)C distance of 5.0 ± 0.3 {\AA}, in agreement with intermolecular hydrogen bonding in a parallel β-sheet structure.",

keywords = "Amino Acid Sequence, Amyloid, Gold, Hydrogen Bonding, Magnetic Resonance Spectroscopy, Metal Nanoparticles, Particle Size, Peptide Fragments, Protein Structure, Secondary, Spectroscopy, Fourier Transform Infrared, Water",

author = "Shaw, {Christopher P} and Middleton, {David A} and Martin Volk and Rapha{\"e}l L{\'e}vy",

year = "2012",

month = feb,

day = "28",

doi = "10.1021/nn204214x",

language = "English",

volume = "6",

pages = "1416--26",

journal = "ACS Nano",

issn = "1936-0851",

publisher = "American Chemical Society",

number = "2",

}

RIS

TY - JOUR

T1 - Amyloid-derived peptide forms self-assembled monolayers on gold nanoparticle with a curvature-dependent β-sheet structure

AU - Shaw, Christopher P

AU - Middleton, David A

AU - Volk, Martin

AU - Lévy, Raphaël

PY - 2012/2/28

Y1 - 2012/2/28

N2 - Using a combination of Fourier transform infrared (FTIR) spectroscopy and solid-state nuclear magnetic resonance (SSNMR) techniques, the secondary structure of peptides anchored on gold nanoparticles of different sizes is investigated. The structure of the well-studied CALNN-capped nanoparticles is compared to the structure of nanoparticles capped with a new cysteine-terminated peptide, CFGAILSS. The design of that peptide is derived from the minimal amyloidogenic sequence FGAIL of the human islet polypeptide amylin. We demonstrate that CFGAILSS forms extended fibrils in solution. When constrained at a nanoparticle surface, CFGAILSS adopts a secondary structure markedly different from CALNN. Taking into account the surface selection rules, the FTIR spectra of CFGAILSS-capped gold nanoparticles indicate the formation of β-sheets which are more prominent for 25 nm diameter nanoparticles than for 5 nm nanoparticles. No intermolecular (13)C-(13)C dipolar coupling is detected with rotational resonance SSNMR for CALNN-capped nanoparticles, while CALNN is in a random coil configuration. Coupling is detected for CFGAILSS-capped gold nanoparticles, however, consistent with an intermolecular (13)C-(13)C distance of 5.0 ± 0.3 Å, in agreement with intermolecular hydrogen bonding in a parallel β-sheet structure.

AB - Using a combination of Fourier transform infrared (FTIR) spectroscopy and solid-state nuclear magnetic resonance (SSNMR) techniques, the secondary structure of peptides anchored on gold nanoparticles of different sizes is investigated. The structure of the well-studied CALNN-capped nanoparticles is compared to the structure of nanoparticles capped with a new cysteine-terminated peptide, CFGAILSS. The design of that peptide is derived from the minimal amyloidogenic sequence FGAIL of the human islet polypeptide amylin. We demonstrate that CFGAILSS forms extended fibrils in solution. When constrained at a nanoparticle surface, CFGAILSS adopts a secondary structure markedly different from CALNN. Taking into account the surface selection rules, the FTIR spectra of CFGAILSS-capped gold nanoparticles indicate the formation of β-sheets which are more prominent for 25 nm diameter nanoparticles than for 5 nm nanoparticles. No intermolecular (13)C-(13)C dipolar coupling is detected with rotational resonance SSNMR for CALNN-capped nanoparticles, while CALNN is in a random coil configuration. Coupling is detected for CFGAILSS-capped gold nanoparticles, however, consistent with an intermolecular (13)C-(13)C distance of 5.0 ± 0.3 Å, in agreement with intermolecular hydrogen bonding in a parallel β-sheet structure.

KW - Amino Acid Sequence

KW - Amyloid

KW - Gold

KW - Hydrogen Bonding

KW - Magnetic Resonance Spectroscopy

KW - Metal Nanoparticles

KW - Particle Size

KW - Peptide Fragments

KW - Protein Structure, Secondary

KW - Spectroscopy, Fourier Transform Infrared

KW - Water

U2 - 10.1021/nn204214x

DO - 10.1021/nn204214x

M3 - Journal article

C2 - 22242947

VL - 6

SP - 1416

EP - 1426

JO - ACS Nano

JF - ACS Nano

SN - 1936-0851

IS - 2

ER -

Research

Text available via DOI:

Keywords