Publication:
Photochemistry and mechanism of designed pyrenyl probe towards promoted cleavage of proteins

0
0

Issued Date

2017

Resource Type

Article

File Type

application/pdf

ISSN

10111344

DOI

10.1016/j.jphotobiol.2017.05.029

Other identifier(s)

2-s2.0-85019926862

Rights Holder(s)

มหาวิทยาลัยศรีนครินทรวิโรฒ

Bibliographic Citation

Journal of Photochemistry and Photobiology B: Biology. Vol 173, (2017), p.35-42

Suggested Citation

Yenjai S., Kuno M., Samosorn S., Liwporncharoenvong T., Buranaprapuk A. Photochemistry and mechanism of designed pyrenyl probe towards promoted cleavage of proteins. Journal of Photochemistry and Photobiology B: Biology. Vol 173, (2017), p.35-42. doi:10.1016/j.jphotobiol.2017.05.029 Retrieved from: https://hdl.handle.net/20.500.14740/4107

Title

Photochemistry and mechanism of designed pyrenyl probe towards promoted cleavage of proteins

Author(s)

Yenjai S.
 Kuno M.
 Samosorn S.
 Liwporncharoenvong T.
 Buranaprapuk A.

Abstract

A new photochemical reagent, succinic acid-1(1-pyrene)methylamide (PMA-SUC), was developed to recognize the specific binding sites on model proteins, egg-white lysozyme and avidin. The interaction of the photochemical reagent with the proteins was studied by UV–Vis, fluorescence spectroscopic methods and docking description. PMA-SUC was found to bind to lysozyme and avidin with binding constants (Kb) of 2.4 × 105 and 6.7 × 105 (M− 1), respectively. The fluorescence intensity of PMA-SUC decreased with increasing concentration of both proteins. Quenching of PMA-SUC fluorescence, in the absence and presence of the protein by an electron acceptor (Hexaamminecobalt(III) chloride, Co(NH3)6Cl3) showed no significant changes in the Ksv values (Stern-Volmer quenching constant), indicating that PMA-SUC bound to the hydrophilic sites or near the surface of the proteins. Irradiation of protein-PMA-SUC mixture, at 342 nm for a period of time, in the presence of Co(NH3)6Cl3 as an electron acceptor, resulted in the cleavage of both proteins with high specificity. Binding mechanisms were studied using Molecular docking method. Molecular docking study indicated the position of PMA-SUC upon binding to the proteins by hydrogen bonding interaction with donor-acceptor within the distance of less than 5 Å in the minimum of binding free energy. The docking results have supported the results obtained from the spectroscopic methods and cleavage studies. © 2017 Elsevier B.V.

Subject(s)

Avidin
 Cobalt chloride
 Egg white
 Lysozyme
 Protein
 Pyrene derivative
 Succinic acid 1 (1 pyrene)methylamide
 Unclassified drug
 Protein binding
 Pyrene
 Pyrene derivative
 Succinic acid derivative
 Succinic acid-1(1-pyrene)methylamide
 Article
 Binding affinity
 Binding site
 Chemical model
 Controlled study
 Electron
 Fluorescence spectroscopy
 Hydrogen bond
 Hydrophilicity
 Molecular docking
 Molecular interaction
 Photochemical quenching
 Photochemistry
 Polyacrylamide gel electrophoresis
 Priority journal
 Protein binding
 Protein cleavage
 Ultraviolet spectrophotometry
 Animal
 Chemistry
 Chicken
 Metabolism
 Photolysis
 Protein tertiary structure
 Radiation response
 Spectrofluorometry
 Synthesis
 Ultraviolet radiation
 Animals
 Avidin
 Binding Sites
 Chickens
 Hydrogen Bonding
 Molecular Docking Simulation
 Muramidase
 Photolysis
 Protein Binding
 Protein Structure, Tertiary
 Pyrenes
 Spectrometry, Fluorescence
 Spectrophotometry, Ultraviolet
 Succinates
 Ultraviolet Rays

View online Resources

Research Projects

Organizational Units

Journal Issue

URI

https://hdl.handle.net/20.500.14740/4107

Collections

Scopus: Year 1983-2021

Endorsement

Review

Supplemented By

Referenced By