4.6 Article

To reveal the nature of interactions of human hemoglobin with gold nanoparticles having two different morphologies (sphere and star-shaped) by using various spectroscopic techniques

期刊

出版社

ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2017.11.026

关键词

Hemoglobin; Gold nanoparticles; Static quenching; Hydrogen bonding; Native secondary structure; Drug-delivery system

资金

  1. University Grant Commission (UGC), New Delhi, India [F.6-6/2014-15/EMERITUS-2014-15-GEN-3976]
  2. DST-SERB project, DST, Govt of India [YSS/2015/000589]

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The nature of interactions between heme protein human hemoglobin (HHb) and gold nanoparticles of two different morphologies that is GNP (spherical) and GNS (star-shaped) have been investigated by using UV-vis absorption, steady state fluorescence, synchronous fluorescence, resonance light scattering (RLS), time resolved fluorescence, FT-IR, and circular dichroism (CD) techniques under physiological condition of pH similar to 7 at ambient and different temperatures. Analysis of the steady state fluorescence quenching of HHb in aqueous solution in the presence of GNP and GNS suggests that the nature of the quenching is of static type. The static nature of the quenching is also confirmed from time resolved data. The static type of quenching also indicates the possibility of formation of ground state complex for both HHb-GNP and HHb-GNS systems. From the measurements of Stern-Volmer (SV) constants K-SV and binding constants, K-A and number of binding sites it appears that HHb forms stronger binding with GNP relative to GNS. Analysis of the thermodynamic parameters indicates that the formation of HHb-GNP and HHb-GNS complexes are spontaneous molecular interaction processes (Delta G < 0). In both cases hydrogen bonding and van der Waals interactions play a dominant role (Delta H < 0, Delta S < 0). Synchronous fluorescence spectroscopy further reveals that the ground state complex formations of HHb-GNP and HHb-GNS preferably occur by binding with the amino acid tyrosine through hydrogen bonding interactions. Moreover the alpha-helicity contents of the proteins as obtained from the circular dichroism (CD) spectra appears to be marginally reduced by increasing concentrations of GNP and GNS and the alpha-helical structures of HHb retain its identity as native secondary structure in spite of complex formations with GNP or GNS. These findings demonstrate the efficiency of biomedical applications of GNP and GNS nanoparticles as well as in elucidating their mechanisms of action as drugs or drug delivery systems in human.

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