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

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

Research output: Chapter in Book/Report/Conference proceedingConference 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 languageEnglish (US)
Title of host publicationOptical Interactions with Tissue and Cells XXVII
PublisherSPIE
Volume9706
ISBN (Electronic)9781628419405
DOIs
StatePublished - 2016
EventOptical Interactions with Tissue and Cells XXVII - San Francisco, United States
Duration: Feb 14 2016Feb 17 2016

Other

OtherOptical Interactions with Tissue and Cells XXVII
CountryUnited States
CitySan Francisco
Period2/14/162/17/16

Keywords

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

ASJC Scopus subject areas

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

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  • Cite this

    Rozinek, S. C., Glickman, R. D., Thomas, R. J., & Brancaleon, L. (2016). Protein-protein binding before and after photo-modification of albumin. In Optical Interactions with Tissue and Cells XXVII (Vol. 9706). [97061J] SPIE. https://doi.org/10.1117/12.2213632