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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

 

Email

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

Biomedical Informatics

 

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.