Author(s): Parimal M Prajapati, Yatri Shah, DJ Sen, CN Patel.

Email(s): prajapati.parimal@yahoo.com , mydream.yatri@gmail.com

DOI: Not Available

Address: Parimal M. Prajapati*, Yatri Shah, D.J. Sen and C.N. Patel
Department of Pharmaceutical and Medicinal Chemistry, Shri Sarvajanik Pharmacy College, Arvind Baug, Mehsana-384001, Gujarat, India.
*Corresponding Author

Published In:   Volume - 2,      Issue - 3,     Year - 2010


ABSTRACT:
Human immunodeficiency virus (HIV) is a lentivirus (a member of the retrovirus family) that causes acquired immunodeficiency syndrome (AIDS), a condition in humans in which the immune system begins to fail, leading to life-threatening opportunistic infections. Infection with HIV occurs by the transfer of blood, semen, vaginal fluid, pre-ejaculate, or breast milk. Within these bodily fluids, HIV is present as both free virus particles and virus within infected immune cells. The four major routes of transmission are unsafe sex, contaminated needles, breast milk, and transmission from an infected mother to her baby at birth. Metallacarboranes derived from the transition metals represent a large family of aromatic borane derivatives which, when equipped with a radiometal, are potentially useful in radioimaging and radiotherapy of tumors. The radiometallacarborane may be localized in tumor by a tumor cell-selective antibody molecule to which it is attached or by other means (biomolecule, liposome). A particular advantage of radiometallacarboranes in these applications is their extraordinarily great kinetic stability and invisibility to enzyme systems which normally degrade organic radiometal carriers (chelates) with release of the radiometal in an unwanted way.


Keywords:

Cite this article:
Parimal M Prajapati, Yatri Shah, DJ Sen, CN Patel. Metallacarboranes: Boron-Based Compounds Inhibit Key HIV Enzyme. Research J. Pharmacology and Pharmacodynamics. 2010; 2(3):205-210.

Cite(Electronic):
Parimal M Prajapati, Yatri Shah, DJ Sen, CN Patel. Metallacarboranes: Boron-Based Compounds Inhibit Key HIV Enzyme. Research J. Pharmacology and Pharmacodynamics. 2010; 2(3):205-210.   Available on: https://rjppd.org/AbstractView.aspx?PID=2010-2-3-11


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