Binding interactions of porphyrin derivatives with Ca(2+) ATPase of sarcoplasmic reticulum (SERCA1a)

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 CaCa(2+) ATPase of sarcoplasmic reticulum (SERCA1a). CAChe software was successfully employed fo...

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Detalles Bibliográficos
Autores principales: Hai, Abdul, Kizilbash, Nadeem A, Zaidi, Syeda Huma H, Alruwaili, Jamal
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2013
Materias:
Hypothesis
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3670123/
https://www.ncbi.nlm.nih.gov/pubmed/23750090
http://dx.doi.org/10.6026/97320630009409
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author Hai, Abdul
Kizilbash, Nadeem A
Zaidi, Syeda Huma H
Alruwaili, Jamal
author_facet Hai, Abdul
Kizilbash, Nadeem A
Zaidi, Syeda Huma H
Alruwaili, Jamal
author_sort Hai, Abdul
collection PubMed
description 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 CaCa(2+) 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 CaCa(2+) ATPase from sarcoplasmic reticulum of rabbit. The results show that FeNOTPPS forms the most stable complex with CaCa(2+) ATPase.
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spelling pubmed-36701232013-06-07 Binding interactions of porphyrin derivatives with Ca(2+) ATPase of sarcoplasmic reticulum (SERCA1a) Hai, Abdul Kizilbash, Nadeem A Zaidi, Syeda Huma H Alruwaili, Jamal Bioinformation Hypothesis 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 CaCa(2+) 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 CaCa(2+) ATPase from sarcoplasmic reticulum of rabbit. The results show that FeNOTPPS forms the most stable complex with CaCa(2+) ATPase. Biomedical Informatics 2013-04-30 /pmc/articles/PMC3670123/ /pubmed/23750090 http://dx.doi.org/10.6026/97320630009409 Text en © 2013 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Hai, Abdul
Kizilbash, Nadeem A
Zaidi, Syeda Huma H
Alruwaili, Jamal
Binding interactions of porphyrin derivatives with Ca(2+) ATPase of sarcoplasmic reticulum (SERCA1a)
title Binding interactions of porphyrin derivatives with Ca(2+) ATPase of sarcoplasmic reticulum (SERCA1a)
title_full Binding interactions of porphyrin derivatives with Ca(2+) ATPase of sarcoplasmic reticulum (SERCA1a)
title_fullStr Binding interactions of porphyrin derivatives with Ca(2+) ATPase of sarcoplasmic reticulum (SERCA1a)
title_full_unstemmed Binding interactions of porphyrin derivatives with Ca(2+) ATPase of sarcoplasmic reticulum (SERCA1a)
title_short Binding interactions of porphyrin derivatives with Ca(2+) ATPase of sarcoplasmic reticulum (SERCA1a)
title_sort binding interactions of porphyrin derivatives with ca(2+) atpase of sarcoplasmic reticulum (serca1a)
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3670123/
https://www.ncbi.nlm.nih.gov/pubmed/23750090
http://dx.doi.org/10.6026/97320630009409
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