PMID- 22410420
OWN - NLM
STAT- MEDLINE
DCOM- 20120703
LR  - 20231004
IS  - 1420-3049 (Electronic)
IS  - 1420-3049 (Linking)
VI  - 17
IP  - 3
DP  - 2012 Mar 12
TI  - Use of spectroscopic, zeta potential and molecular dynamic techniques to study 
      the interaction between human holo-transferrin and two antagonist drugs: 
      comparison of binary and ternary systems.
PG  - 3114-47
LID - 10.3390/molecules17033114 [doi]
AB  - For the first time, the binding of ropinirole hydrochloride (ROP) and aspirin 
      (ASA) to human holo-transferrin (hTf) has been investigated by spectroscopic 
      approaches (fluorescence quenching, synchronous fluorescence, time-resolved 
      fluorescence, three-dimensional fluorescence, UV-vis absorption, circular 
      dichroism, resonance light scattering), as well as zeta potential and molecular 
      modeling techniques, under simulated physiological conditions. Fluorescence 
      analysis was used to estimate the effect of the ROP and ASA drugs on the 
      fluorescence of hTf as well as to define the binding and quenching properties of 
      binary and ternary complexes. The synchronized fluorescence and three-dimensional 
      fluorescence spectra demonstrated some micro-environmental and conformational 
      changes around the Trp and Tyr residues with a faint red shift. Thermodynamic 
      analysis displayed the van der Waals forces and hydrogen bonds interactions are 
      the major acting forces in stabilizing the complexes. Steady-state and 
      time-resolved fluorescence data revealed that the fluorescence quenching of 
      complexes are static mechanism. The effect of the drugs aggregating on the hTf 
      resulted in an enhancement of the resonance light scattering (RLS) intensity. The 
      average binding distance between were computed according to the forster 
      non-radiation energy transfer theory. The circular dichroism (CD) spectral 
      examinations indicated that the binding of the drugs induced a conformational 
      change of hTf. Measurements of the zeta potential indicated that the combination 
      of electrostatic and hydrophobic interactions between ROP, ASA and hTf formed 
      micelle-like clusters. The molecular modeling confirmed the experimental results. 
      This study is expected to provide important insight into the interaction of hTf 
      with ROP and ASA to use in various toxicological and therapeutic processes.
FAU - Kabiri, Mona
AU  - Kabiri M
AD  - Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad 
      University, Mashhad 9175687119, Iran.
FAU - Amiri-Tehranizadeh, Zeinab
AU  - Amiri-Tehranizadeh Z
FAU - Baratian, Ali
AU  - Baratian A
FAU - Saberi, Mohammad Reza
AU  - Saberi MR
FAU - Chamani, Jamshidkhan
AU  - Chamani J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20120312
PL  - Switzerland
TA  - Molecules
JT  - Molecules (Basel, Switzerland)
JID - 100964009
RN  - 0 (Indoles)
RN  - 0 (Transferrin)
RN  - 030PYR8953 (ropinirole)
RN  - R16CO5Y76E (Aspirin)
SB  - IM
MH  - Algorithms
MH  - Aspirin/*chemistry
MH  - Binding Sites
MH  - Circular Dichroism
MH  - Fluorescence Resonance Energy Transfer
MH  - Humans
MH  - Hydrogen Bonding
MH  - Hydrophobic and Hydrophilic Interactions
MH  - Indoles/*chemistry
MH  - Light
MH  - *Molecular Dynamics Simulation
MH  - Protein Binding
MH  - Protein Structure, Secondary
MH  - Scattering, Radiation
MH  - Spectrometry, Fluorescence
MH  - Thermodynamics
MH  - Transferrin/antagonists & inhibitors/*chemistry
PMC - PMC6268275
EDAT- 2012/03/14 06:00
MHDA- 2012/07/04 06:00
PMCR- 2012/03/12
CRDT- 2012/03/14 06:00
PHST- 2011/12/01 00:00 [received]
PHST- 2012/02/24 00:00 [revised]
PHST- 2012/02/28 00:00 [accepted]
PHST- 2012/03/14 06:00 [entrez]
PHST- 2012/03/14 06:00 [pubmed]
PHST- 2012/07/04 06:00 [medline]
PHST- 2012/03/12 00:00 [pmc-release]
AID - molecules17033114 [pii]
AID - molecules-17-03114 [pii]
AID - 10.3390/molecules17033114 [doi]
PST - epublish
SO  - Molecules. 2012 Mar 12;17(3):3114-47. doi: 10.3390/molecules17033114.