Infrared ellipsometry studies of thermal stability of protein monolayers and multilayers

H. Arwin; A. Askendahl; P. Tengvall; D. W. Thompson; J. A. Woollam

doi:10.1002/pssc.200777898

Infrared ellipsometry studies of thermal stability of protein monolayers and multilayers

H. Arwin, A. Askendahl, P. Tengvall, D. W. Thompson, J. A. Woollam

Research output: Contribution to journal › Conference article › peer-review

11 Scopus citations

Abstract

Methodology for studies of effects of heating multilayers of human serum albumin (HSA) and anti-HSA is presented. Multilayers of anti-HSA were prepared on silicon substrates and studied with infrared spectroscopic ellipsometry equipped with a heat stage. The refractive index N = n+ik and the layer thickness are determined and the amide bands are analyzed. It is found that HSA/anti-HSA multilayers are stable for shorter times at temperatures above 100 °C, except for small thickness changes. Also pilot studies of effects of heating monolayers of proteins adsorbed on gold substrates is presented.

Original language	English (US)
Pages (from-to)	1438-1441
Number of pages	4
Journal	Physica Status Solidi (C) Current Topics in Solid State Physics
Volume	5
Issue number	5
DOIs	https://doi.org/10.1002/pssc.200777898
State	Published - 2008
Externally published	Yes
Event	4th International Conference on Spectroscopic Ellipsometry, ICSE4 - Stockholm, Sweden Duration: Jun 11 2007 → Jun 15 2007

ASJC Scopus subject areas

Condensed Matter Physics

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10.1002/pssc.200777898

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title = "Infrared ellipsometry studies of thermal stability of protein monolayers and multilayers",

abstract = "Methodology for studies of effects of heating multilayers of human serum albumin (HSA) and anti-HSA is presented. Multilayers of anti-HSA were prepared on silicon substrates and studied with infrared spectroscopic ellipsometry equipped with a heat stage. The refractive index N = n+ik and the layer thickness are determined and the amide bands are analyzed. It is found that HSA/anti-HSA multilayers are stable for shorter times at temperatures above 100 °C, except for small thickness changes. Also pilot studies of effects of heating monolayers of proteins adsorbed on gold substrates is presented.",

author = "H. Arwin and A. Askendahl and P. Tengvall and Thompson, {D. W.} and Woollam, {J. A.}",

year = "2008",

doi = "10.1002/pssc.200777898",

language = "English (US)",

volume = "5",

pages = "1438--1441",

journal = "Physica Status Solidi (C) Current Topics in Solid State Physics",

issn = "1862-6351",

publisher = "Wiley-VCH Verlag",

number = "5",

note = "4th International Conference on Spectroscopic Ellipsometry, ICSE4 ; Conference date: 11-06-2007 Through 15-06-2007",

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TY - JOUR

T1 - Infrared ellipsometry studies of thermal stability of protein monolayers and multilayers

AU - Arwin, H.

AU - Askendahl, A.

AU - Tengvall, P.

AU - Thompson, D. W.

AU - Woollam, J. A.

PY - 2008

Y1 - 2008

N2 - Methodology for studies of effects of heating multilayers of human serum albumin (HSA) and anti-HSA is presented. Multilayers of anti-HSA were prepared on silicon substrates and studied with infrared spectroscopic ellipsometry equipped with a heat stage. The refractive index N = n+ik and the layer thickness are determined and the amide bands are analyzed. It is found that HSA/anti-HSA multilayers are stable for shorter times at temperatures above 100 °C, except for small thickness changes. Also pilot studies of effects of heating monolayers of proteins adsorbed on gold substrates is presented.

AB - Methodology for studies of effects of heating multilayers of human serum albumin (HSA) and anti-HSA is presented. Multilayers of anti-HSA were prepared on silicon substrates and studied with infrared spectroscopic ellipsometry equipped with a heat stage. The refractive index N = n+ik and the layer thickness are determined and the amide bands are analyzed. It is found that HSA/anti-HSA multilayers are stable for shorter times at temperatures above 100 °C, except for small thickness changes. Also pilot studies of effects of heating monolayers of proteins adsorbed on gold substrates is presented.

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DO - 10.1002/pssc.200777898

M3 - Conference article

AN - SCOPUS:77951145402

SN - 1862-6351

VL - 5

SP - 1438

EP - 1441

JO - Physica Status Solidi (C) Current Topics in Solid State Physics

JF - Physica Status Solidi (C) Current Topics in Solid State Physics

IS - 5

T2 - 4th International Conference on Spectroscopic Ellipsometry, ICSE4

Y2 - 11 June 2007 through 15 June 2007

ER -

Infrared ellipsometry studies of thermal stability of protein monolayers and multilayers

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