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Behavior of β-amyloid 1-16 at the air-water interface at varying ph by nonlinear spectroscopy and molecular dynamics simulations

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Behavior of β-amyloid 1-16 at the air-water interface at varying ph by nonlinear spectroscopy and molecular dynamics simulations. / Miller, Abigail E.; Petersen, Poul B.; Hollars, Christopher W.; Saykally, Richard J.; Heyda, Jan; Jungwirth, Pavel.

In: Journal of Physical Chemistry A, Vol. 115, No. 23, 16.06.2011, p. 5873-5880.

Research output: Contribution to journalArticleScientificpeer-review

Harvard

Miller, AE, Petersen, PB, Hollars, CW, Saykally, RJ, Heyda, J & Jungwirth, P 2011, 'Behavior of β-amyloid 1-16 at the air-water interface at varying ph by nonlinear spectroscopy and molecular dynamics simulations', Journal of Physical Chemistry A, vol. 115, no. 23, pp. 5873-5880. https://doi.org/10.1021/jp110103j

APA

Miller, A. E., Petersen, P. B., Hollars, C. W., Saykally, R. J., Heyda, J., & Jungwirth, P. (2011). Behavior of β-amyloid 1-16 at the air-water interface at varying ph by nonlinear spectroscopy and molecular dynamics simulations. Journal of Physical Chemistry A, 115(23), 5873-5880. https://doi.org/10.1021/jp110103j

Vancouver

Miller AE, Petersen PB, Hollars CW, Saykally RJ, Heyda J, Jungwirth P. Behavior of β-amyloid 1-16 at the air-water interface at varying ph by nonlinear spectroscopy and molecular dynamics simulations. Journal of Physical Chemistry A. 2011 Jun 16;115(23):5873-5880. https://doi.org/10.1021/jp110103j

Author

Miller, Abigail E. ; Petersen, Poul B. ; Hollars, Christopher W. ; Saykally, Richard J. ; Heyda, Jan ; Jungwirth, Pavel. / Behavior of β-amyloid 1-16 at the air-water interface at varying ph by nonlinear spectroscopy and molecular dynamics simulations. In: Journal of Physical Chemistry A. 2011 ; Vol. 115, No. 23. pp. 5873-5880.

Bibtex - Download

@article{3fdff033104344db834d5f2daa855665,
title = "Behavior of β-amyloid 1-16 at the air-water interface at varying ph by nonlinear spectroscopy and molecular dynamics simulations",
abstract = "The adsorption and aggregation of β-amyloid (1-16) fragment at the air-water interface was investigated by the combination of second harmonic generation (SHG) spectroscopy, Brewster angle microscopy (BAM), and molecular dynamics simulations (MD). The Gibbs free energy of surface adsorption was measured to be -10.3 kcal/mol for bulk pHs of 7.4 and 3, but no adsorption was observed for pH 10-11. The 1-16 fragment is believed not to be involved in fibril formation of the β-amyloid protein, but it exhibits interesting behavior at the air-water interface, as manifested in two time scales for the observed SHG response. The shorter time scale (minutes) reflects the surface adsorption, and the longer time scale (hours) reflects rearrangement and aggregation of the peptide at the air-water interface. Both of these processes are also evidenced by BAM measurements.MDsimulations confirm the pH dependence of surface behavior of the β-amyloid, with largest surface affinity found at pH = 7. It also follows from the simulations that phenylalanine is the most surface exposed residue, followed by tyrosine and histidine in their neutral form.",
author = "Miller, {Abigail E.} and Petersen, {Poul B.} and Hollars, {Christopher W.} and Saykally, {Richard J.} and Jan Heyda and Pavel Jungwirth",
year = "2011",
month = "6",
day = "16",
doi = "10.1021/jp110103j",
language = "English",
volume = "115",
pages = "5873--5880",
journal = "Journal of Physical Chemistry A",
issn = "1089-5639",
publisher = "American Chemical Society",
number = "23",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Behavior of β-amyloid 1-16 at the air-water interface at varying ph by nonlinear spectroscopy and molecular dynamics simulations

AU - Miller, Abigail E.

AU - Petersen, Poul B.

AU - Hollars, Christopher W.

AU - Saykally, Richard J.

AU - Heyda, Jan

AU - Jungwirth, Pavel

PY - 2011/6/16

Y1 - 2011/6/16

N2 - The adsorption and aggregation of β-amyloid (1-16) fragment at the air-water interface was investigated by the combination of second harmonic generation (SHG) spectroscopy, Brewster angle microscopy (BAM), and molecular dynamics simulations (MD). The Gibbs free energy of surface adsorption was measured to be -10.3 kcal/mol for bulk pHs of 7.4 and 3, but no adsorption was observed for pH 10-11. The 1-16 fragment is believed not to be involved in fibril formation of the β-amyloid protein, but it exhibits interesting behavior at the air-water interface, as manifested in two time scales for the observed SHG response. The shorter time scale (minutes) reflects the surface adsorption, and the longer time scale (hours) reflects rearrangement and aggregation of the peptide at the air-water interface. Both of these processes are also evidenced by BAM measurements.MDsimulations confirm the pH dependence of surface behavior of the β-amyloid, with largest surface affinity found at pH = 7. It also follows from the simulations that phenylalanine is the most surface exposed residue, followed by tyrosine and histidine in their neutral form.

AB - The adsorption and aggregation of β-amyloid (1-16) fragment at the air-water interface was investigated by the combination of second harmonic generation (SHG) spectroscopy, Brewster angle microscopy (BAM), and molecular dynamics simulations (MD). The Gibbs free energy of surface adsorption was measured to be -10.3 kcal/mol for bulk pHs of 7.4 and 3, but no adsorption was observed for pH 10-11. The 1-16 fragment is believed not to be involved in fibril formation of the β-amyloid protein, but it exhibits interesting behavior at the air-water interface, as manifested in two time scales for the observed SHG response. The shorter time scale (minutes) reflects the surface adsorption, and the longer time scale (hours) reflects rearrangement and aggregation of the peptide at the air-water interface. Both of these processes are also evidenced by BAM measurements.MDsimulations confirm the pH dependence of surface behavior of the β-amyloid, with largest surface affinity found at pH = 7. It also follows from the simulations that phenylalanine is the most surface exposed residue, followed by tyrosine and histidine in their neutral form.

UR - http://www.scopus.com/inward/record.url?scp=79959981055&partnerID=8YFLogxK

U2 - 10.1021/jp110103j

DO - 10.1021/jp110103j

M3 - Article

VL - 115

SP - 5873

EP - 5880

JO - Journal of Physical Chemistry A

JF - Journal of Physical Chemistry A

SN - 1089-5639

IS - 23

ER -