Protein-protein binding before and after photo-modification of albumin

Sarah C. Rozinek; Randolph D. Glickman; Robert J. Thomas; Lorenzo Brancaleon

doi:10.1117/12.2213632

Protein-protein binding before and after photo-modification of albumin

Sarah C. Rozinek, Randolph D. Glickman, Robert J. Thomas, Lorenzo Brancaleon

Ophthalmology

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

Abstract

Bioeffects of directed-optical-energy encompass a wide range of applications. One aspect of photochemical interactions involves irradiating a photosensitizer with visible light in order to induce protein unfolding and consequent changes in function. In the past, irradiation of several dye-protein combinations has revealed effects on protein structure. Beta lactoglobulin, human serum albumin (HSA) and tubulin have all been photo-modified with meso-tetrakis(4-sulfonatophenyl)porphyrin (TSPP) bound, but only in the case of tubulin has binding caused a verified loss of biological function (loss of ability to form microtubules) as a result of this light-induced structural change. The current work questions if the photo-induced structural changes that occur to HSA, are sufficient to disable its biological function of binding to osteonectin. The albumin-binding protein, osteonectin, is about half the molecular weight of HSA, so the two proteins and their bound product can be separated and quantified by size exclusion high performance liquid chromatography. TSPP was first bound to HSA and irradiated, photo-modifying the structure of HSA. Then native HSA or photo-modified HSA (both with TSPP bound) were compared, to assess loss in HSA's innate binding ability as a result of light-induced structure modification.

Original language	English (US)
Title of host publication	Optical Interactions with Tissue and Cells XXVII
Editors	E. Duco Jansen
Publisher	SPIE
ISBN (Electronic)	9781628419405
DOIs	https://doi.org/10.1117/12.2213632
State	Published - 2016
Event	Optical Interactions with Tissue and Cells XXVII - San Francisco, United States Duration: Feb 14 2016 → Feb 17 2016

Publication series

Name	Progress in Biomedical Optics and Imaging - Proceedings of SPIE
Volume	9706
ISSN (Print)	1605-7422

Other

Other	Optical Interactions with Tissue and Cells XXVII
Country	United States
City	San Francisco
Period	2/14/16 → 2/17/16

Keywords

HPLC
HSA
SPARC
albumin
osteonectin
photosensitizer
protein-protein binding
size exclusion chromatography

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
Biomaterials
Atomic and Molecular Physics, and Optics
Radiology Nuclear Medicine and imaging

Access to Document

10.1117/12.2213632

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Protein-protein binding before and after photo-modification of albumin. / Rozinek, Sarah C.; Glickman, Randolph D.; Thomas, Robert J.; Brancaleon, Lorenzo.

Optical Interactions with Tissue and Cells XXVII. ed. / E. Duco Jansen. SPIE, 2016. 97061J (Progress in Biomedical Optics and Imaging - Proceedings of SPIE; Vol. 9706).

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

Rozinek, SC, Glickman, RD, Thomas, RJ & Brancaleon, L 2016, Protein-protein binding before and after photo-modification of albumin. in ED Jansen (ed.), Optical Interactions with Tissue and Cells XXVII., 97061J, Progress in Biomedical Optics and Imaging - Proceedings of SPIE, vol. 9706, SPIE, Optical Interactions with Tissue and Cells XXVII, San Francisco, United States, 2/14/16. https://doi.org/10.1117/12.2213632

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title = "Protein-protein binding before and after photo-modification of albumin",

abstract = "Bioeffects of directed-optical-energy encompass a wide range of applications. One aspect of photochemical interactions involves irradiating a photosensitizer with visible light in order to induce protein unfolding and consequent changes in function. In the past, irradiation of several dye-protein combinations has revealed effects on protein structure. Beta lactoglobulin, human serum albumin (HSA) and tubulin have all been photo-modified with meso-tetrakis(4-sulfonatophenyl)porphyrin (TSPP) bound, but only in the case of tubulin has binding caused a verified loss of biological function (loss of ability to form microtubules) as a result of this light-induced structural change. The current work questions if the photo-induced structural changes that occur to HSA, are sufficient to disable its biological function of binding to osteonectin. The albumin-binding protein, osteonectin, is about half the molecular weight of HSA, so the two proteins and their bound product can be separated and quantified by size exclusion high performance liquid chromatography. TSPP was first bound to HSA and irradiated, photo-modifying the structure of HSA. Then native HSA or photo-modified HSA (both with TSPP bound) were compared, to assess loss in HSA's innate binding ability as a result of light-induced structure modification.",

keywords = "HPLC, HSA, SPARC, albumin, osteonectin, photosensitizer, protein-protein binding, size exclusion chromatography",

author = "Rozinek, {Sarah C.} and Glickman, {Randolph D.} and Thomas, {Robert J.} and Lorenzo Brancaleon",

note = "Funding Information: S.C.R is supported by the Consortium Research Fellows Program (FA8650-13-2-6333). The research is funded by a combination of an AFOSR grant (FA8650-07-D-6800) to R.J.T. and an NIH grant (G12RR013646-1) to L.B. Additionally, S.C.R. wishes to thank the co-authors of this work, as well as Morgan Schmidt (Engility) for their research. Pending Distribution A: Approved for public release; distribution unlimited. STINFO PA Case No: RH-16-115075; Optical Interactions with Tissue and Cells XXVII ; Conference date: 14-02-2016 Through 17-02-2016",

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AU - Rozinek, Sarah C.

AU - Glickman, Randolph D.

AU - Thomas, Robert J.

AU - Brancaleon, Lorenzo

N1 - Funding Information: S.C.R is supported by the Consortium Research Fellows Program (FA8650-13-2-6333). The research is funded by a combination of an AFOSR grant (FA8650-07-D-6800) to R.J.T. and an NIH grant (G12RR013646-1) to L.B. Additionally, S.C.R. wishes to thank the co-authors of this work, as well as Morgan Schmidt (Engility) for their research. Pending Distribution A: Approved for public release; distribution unlimited. STINFO PA Case No: RH-16-115075

PY - 2016

Y1 - 2016

N2 - Bioeffects of directed-optical-energy encompass a wide range of applications. One aspect of photochemical interactions involves irradiating a photosensitizer with visible light in order to induce protein unfolding and consequent changes in function. In the past, irradiation of several dye-protein combinations has revealed effects on protein structure. Beta lactoglobulin, human serum albumin (HSA) and tubulin have all been photo-modified with meso-tetrakis(4-sulfonatophenyl)porphyrin (TSPP) bound, but only in the case of tubulin has binding caused a verified loss of biological function (loss of ability to form microtubules) as a result of this light-induced structural change. The current work questions if the photo-induced structural changes that occur to HSA, are sufficient to disable its biological function of binding to osteonectin. The albumin-binding protein, osteonectin, is about half the molecular weight of HSA, so the two proteins and their bound product can be separated and quantified by size exclusion high performance liquid chromatography. TSPP was first bound to HSA and irradiated, photo-modifying the structure of HSA. Then native HSA or photo-modified HSA (both with TSPP bound) were compared, to assess loss in HSA's innate binding ability as a result of light-induced structure modification.

AB - Bioeffects of directed-optical-energy encompass a wide range of applications. One aspect of photochemical interactions involves irradiating a photosensitizer with visible light in order to induce protein unfolding and consequent changes in function. In the past, irradiation of several dye-protein combinations has revealed effects on protein structure. Beta lactoglobulin, human serum albumin (HSA) and tubulin have all been photo-modified with meso-tetrakis(4-sulfonatophenyl)porphyrin (TSPP) bound, but only in the case of tubulin has binding caused a verified loss of biological function (loss of ability to form microtubules) as a result of this light-induced structural change. The current work questions if the photo-induced structural changes that occur to HSA, are sufficient to disable its biological function of binding to osteonectin. The albumin-binding protein, osteonectin, is about half the molecular weight of HSA, so the two proteins and their bound product can be separated and quantified by size exclusion high performance liquid chromatography. TSPP was first bound to HSA and irradiated, photo-modifying the structure of HSA. Then native HSA or photo-modified HSA (both with TSPP bound) were compared, to assess loss in HSA's innate binding ability as a result of light-induced structure modification.

KW - HPLC

KW - HSA

KW - SPARC

KW - albumin

KW - osteonectin

KW - photosensitizer

KW - protein-protein binding

KW - size exclusion chromatography

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