Title |
Binding interactions of porphyrin derivatives with Ca2+ ATPase of sarcoplasmic reticulum (SERCA1a)
|
Authors |
Abdul Hai1, Nadeem A. Kizilbash1*, Syeda Huma H. Zaidiand2 & Jamal Alruwaili1
|
Affiliation |
1Department of Biochemistry, Faculty of Medicine and Applied Medical Sciences; 2Department of Chemistry, Faculty of Science,Northern Border University, P.O. Box 1321, Arar-91431, Saudi Arabia |
|
nadeem_kizilbash@yahoo.com; *Corresponding author |
Article Type |
Hypothesis |
Date |
Received March 30, 2013; Accepted April 05, 2013; Published April 30, 2013
|
Abstract |
The use of Porphyrin derivatives as photosensitizers in Photodynamic Therapy (PDT) was investigated by means of a molecular docking study. These molecules can bind to intracellular targets such as P-type Ca2+ ATPase of sarcoplasmic reticulum (SERCA1a). CAChe software was successfully employed for conducting the docking of Tetraphenylporphinesulfonate(TPPS), 5,10,15,20-Tetrakis (4-sulfonatophenyl) porphyrinato Iron(III) Chloride (FeTPPS) and 5,10,15,20-Tetrakis (4-sulfonatophenyl) porphyrinato Iron(III) nitrosyl Chloride (FeNOTPPS) with Ca2+ ATPase from sarcoplasmic reticulum of rabbit. The results show that FeNOTPPS forms the most stable complex with Ca2+ ATPase.
|
Keywords |
Porphyrin derivatives, Molecular docking, Photodynamic therapy, Photosensitizers.
|
Citation |
Hai et al.
Bioinformation 9(8): 409-413 (2013) |
Edited by |
P Kangueane
|
ISSN |
0973-2063
|
Publisher |
|
License |
This is an Open Access article which permits unrestricted use,
distribution, and reproduction in any medium, provided the original
work is properly credited. This is distributed under the terms of
the
Creative Commons Attribution License. |