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Photophysics of a proton transfer phototautomer within biological confinement of a protein: Spectroscopic and molecular docking studies
Published in Elsevier
Volume: 153
Pages: 430 - 438
The present work demonstrates the effect of biological confinement on the photophysics of a proton transfer phototautomer viz.; 2-hydroxy-1-naphthaldehyde (HN21). HN21 is a potential candidate exhibiting excited-state intramolecular proton transfer (ESIPT) reaction and thereby generating the phototautomer (i.e.; proton transferred keto form) in the excited-state. The ESIPT photophysics of the probe (HN21) is found to be remarkably modified within the confined bio-environment of a model transport protein Bovine Serum Albumin (BSA). Such considerable modification of the ESIPT photophysics of the probe has been exploited to determine the probe-protein binding strength (binding constant, K(±10%)=1.23×104 M-1). The probe-protein binding process is found to be thermodynamically feasible (ΔG=-24.25 kJ mol-1). The present work also delves into evaluation of the probable binding location of the probe (HN21) within the biomacromolecular assembly of the protein by blind docking simulation technique, which reveals that HN21 favorably binds to the hydrophobic subdomain IIIA of BSA. Circular dichroism (CD) spectroscopy delineates the effect of probe binding on the protein secondary structure in terms of decrease of α-helical content of BSA with increasing probe concentration. Apart from this, excitation-emission matrix fluorescence technique is found to hint at the effect on protein tertiary structure upon binding to the probe. The modulated dynamics of the proton transfer phototautomer of HN21 within the biological confinement is investigated in this context by time-resolved fluorescence decay measurements. The present work also accentuates the mutually corroborating data found from experimental and computational studies. © 2014 Elsevier B.V.
About the journal
JournalData powered by TypesetJournal of Luminescence
PublisherData powered by TypesetElsevier
Open AccessNo