Interaction between holo transferrin and HSA–PPIX complex in the presence of lomefloxacin: An evaluation of PPIX aggregation in protein–protein interactions
Author:
, , , , , ,Year
: 2012
Abstract: Human serum albumin (HSA) and holo transferrin (TF) are two serum carrier proteins that are able to
interact with each other, thereby altering their binding behavior toward their ligands. During the course
of this study, the interaction between HSA–PPIX and TF, in the presence and absence of lomefloxacin
(LMF), was for the first time investigated using different spectroscopic and molecular modeling techniques.
Fluorescence spectroscopy experiments were performed in order to study conformational
changes of proteins. The RLS technique was utilized to investigate the effect of LMF on J-aggregation of
PPIX, which is the first report of its kind. Our findings present clear-cut evidence for the alteration of
interactions between HSA and TF in the presence of PPIX and changes in drug-binding to HSA and
HSA–PPIX complex upon interaction with TF. Moreover, molecular modeling studies suggested that the
binding site for LMF became switched in the presence of PPIX, and that LMF bound to the site IIA of
HSA. The obtained results should give new insight into research in this field and may cast some light
on the dynamics of drugs in biological systems.
interact with each other, thereby altering their binding behavior toward their ligands. During the course
of this study, the interaction between HSA–PPIX and TF, in the presence and absence of lomefloxacin
(LMF), was for the first time investigated using different spectroscopic and molecular modeling techniques.
Fluorescence spectroscopy experiments were performed in order to study conformational
changes of proteins. The RLS technique was utilized to investigate the effect of LMF on J-aggregation of
PPIX, which is the first report of its kind. Our findings present clear-cut evidence for the alteration of
interactions between HSA and TF in the presence of PPIX and changes in drug-binding to HSA and
HSA–PPIX complex upon interaction with TF. Moreover, molecular modeling studies suggested that the
binding site for LMF became switched in the presence of PPIX, and that LMF bound to the site IIA of
HSA. The obtained results should give new insight into research in this field and may cast some light
on the dynamics of drugs in biological systems.
Keyword(s): HSA
Holo transferrin
Fluorescence quenching
Zeta-potential
Protein–protein interaction
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Interaction between holo transferrin and HSA–PPIX complex in the presence of lomefloxacin: An evaluation of PPIX aggregation in protein–protein interactions
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| contributor author | Zohreh Sattar | en |
| contributor author | Hediye Iranfar | en |
| contributor author | احمد آسوده | en |
| contributor author | Mohammad Reza Saberi | en |
| contributor author | Mahboobeh Mazhari | en |
| contributor author | Jamshidkhan Chamani | en |
| contributor author | Ahmad Asoodeh | fa |
| date accessioned | 2020-06-06T13:09:04Z | |
| date available | 2020-06-06T13:09:04Z | |
| date issued | 2012 | |
| identifier uri | https://libsearch.um.ac.ir:443/fum/handle/fum/3343581?locale-attribute=en | |
| description abstract | Human serum albumin (HSA) and holo transferrin (TF) are two serum carrier proteins that are able to interact with each other, thereby altering their binding behavior toward their ligands. During the course of this study, the interaction between HSA–PPIX and TF, in the presence and absence of lomefloxacin (LMF), was for the first time investigated using different spectroscopic and molecular modeling techniques. Fluorescence spectroscopy experiments were performed in order to study conformational changes of proteins. The RLS technique was utilized to investigate the effect of LMF on J-aggregation of PPIX, which is the first report of its kind. Our findings present clear-cut evidence for the alteration of interactions between HSA and TF in the presence of PPIX and changes in drug-binding to HSA and HSA–PPIX complex upon interaction with TF. Moreover, molecular modeling studies suggested that the binding site for LMF became switched in the presence of PPIX, and that LMF bound to the site IIA of HSA. The obtained results should give new insight into research in this field and may cast some light on the dynamics of drugs in biological systems. | en |
| language | English | |
| title | Interaction between holo transferrin and HSA–PPIX complex in the presence of lomefloxacin: An evaluation of PPIX aggregation in protein–protein interactions | en |
| type | Journal Paper | |
| contenttype | External Fulltext | |
| subject keywords | HSA Holo transferrin Fluorescence quenching Zeta-potential Protein–protein interaction | en |
| journal title | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | fa |
| pages | 1089-1100 | |
| journal volume | 98 | |
| journal issue | 8 | |
| identifier link | https://profdoc.um.ac.ir/paper-abstract-1029263.html | |
| identifier articleid | 1029263 |