Effects of Visible‐Light Irradiation of Protoporphyrin IX on the Self‐Assembly of Tubulin Heterodimers

Abstract

The formation and the effects of laser irradiation of the complex formed by protoporphyrin IX (PPIX) and tubulin was investigated. We have used tubulin as a model protein to investigate whether docked photoactive ligands can affect the structure and function of polypeptides upon exposure to visible light. We observed that laser irradiation in the Soret band prompts bleaching of the PPIX, which is accompanied by a sharp decrease in the intensity and average fluorescence lifetime of the protein (dominated by the four tryptophan residues of the tubulin monomer). The kinetics indicate non‐trivial effects and suggest that the photosensitization of the PPIX bound to tubulin prompts structural alterations of the protein. These modifications were also observed through changes in the energy transfer between Trp residues and PPIX. The results suggest that laser irradiation produces localized partial unfolding of tubulin and that the changes prompt modification of the formation of microtubules in vitro. Measurements of singlet oxygen formation were inconclusive in determining whether the changes are prompted by reactive oxygen species or other excited state mechanisms.

Document Details

Document Type
Pub Defense Publication
Publication Date
Aug 30, 2016
Source ID
10.1002/cphc.201600629

Entities

People

  • Alicia Vall‐sagarra
  • Brady Mcmicken
  • Lorenzo Brancaleon
  • Santi Nonell

Organizations

  • National Institutes of Health
  • University Ramon Llull
  • University of Texas at San Antonio

Tags

Fields of Study

  • Chemistry

Readers

  • Chemistry (specifically Chemical Fluorescence)
  • Molecular and Cellular Biochemistry

Technology Areas

  • Directed Energy
  • Directed Energy - Lasers