Spectrophotometric studies on the effect of two porphyrin compounds on structure and binding of human serum albumin.

Ajloo, Davood and Teimoortash, Ali Reza and Zakavi, Saeed and Asadzadeh, Mona and Evini, Mina and Saboury, Ali Akbar and Moosavi-Movahedi, Ali Akbar (2008) Spectrophotometric studies on the effect of two porphyrin compounds on structure and binding of human serum albumin. In: 11th Iranian Physical Chemistry Seminar-July 2008.

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Abstract

Effect of two porphyrin; meso-tetrakis(4-sulphotanophenyl)porphyrin (H2TPPS4) and meso-tetrakis(3-sulphonato-4-methoxyphenyl)porphyrin (H2TAPS4) on the structure of human serum albumin (HSA) were investigated by UV-Vis spectrophotometery, circular dichroism (CD) fluorescence spectrophotometery and GROMACS molecular dynamics (MD) in different temperature (17, 27 and 37oC), different pH (6.5, 7.5 and 8.5) and different ionic strength (10 mM, 50 mM and 100 mM). The results show that increasing the pH and ionic strength decreases the binding. Increasing the temperature do not show the regular trend. The spectrophotometric results (CD and fluorescence) indicate that, both ligands unfolded the protein (decreasing the secondary and tertiary structure). The effect of H2TAPS4 on the midpoint transition temperature (Tm ) of HSA was investigated by fluorescence in different pH. It is resulted that HSA is more unfolded and less stable in lower pH.

Item Type: Conference or Workshop Item (Poster)
Persian Title: Spectrophotometric studies on the effect of two porphyrin compounds on structure and binding of human serum albumin.
Persian Abstract: -
Subjects: Divisions > Conferences > 11th Iranian Physical Chemistry Seminar- July 2008
Conferences > 11th Iranian Physical Chemistry Seminar- July 2008
Divisions: Conferences > 11th Iranian Physical Chemistry Seminar- July 2008
Subjects > Conferences > 11th Iranian Physical Chemistry Seminar- July 2008
Date Deposited: 17 Jun 2019 05:08
Last Modified: 17 Jun 2019 05:08
URI: http://repository.uma.ac.ir/id/eprint/6801

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