is necessary for the domain to be functional and for the stabilization of the conformation of the structure, allowing the NCp7 to carry out the processes required for HIV replication. Since the CCHC binding site is mutation resistant and involved in the replication of HIV-1, it makes a prime candidate for the prevention of HIV through zinc ejectors. By inhibiting the function of NCp7, the viral replication is affected and a non-functional virus that is unable to infect its host is produced. Zinc Ejector Compounds Azodicarbonamide Azodicarbonamide (ADA) was the first zinc ejector to go into clinical trial for treatment of HIV. ADA inhibits HIV by electrophilically attacking the sulfur atoms of the zinc coordinated cysteine. This electrophilic interaction destabilizes the zinc binding site making it easier for the zinc ion to be withdrawn due to the new arrangement of bonds. The binding site then performs a disulfide exchange, forming new intermolecular disulfide bonds, and rearrangement occurs placing the zinc finger in a conformation that inhibits its function. C-nitroso 3-nitrosobenzamide (NOBA) and 6-nitroso-1,2-benzopyrone (NOBP) were the first compounds to demonstrate an ability to inhibit infection of HIV by ejecting zinc from NCp7. In the same manner as ADA, the compounds interact with an 18-residue polypeptide on the N terminal zinc knuckle region of the HIV nucleocapsid protein which causes ejection of the zinc from the region by covalently modifying the cysteine residues. Studies suggest that NOBA and NOBP were able to inhibit HIV-1 infection by inhibiting reverse transcription without an apparent impairment of reverse transcriptase. This reiterates the role of NCp7 in reverse transcription. 2,2’-di-thiobisbenzamide (DIBA) DIBAs act similarly to ADA, NOBA and NOBP. They react with the cysteine residues on the zinc finger of the NCp7 and cause a covalent conformation change which ejects the zinc from the zinc finger domain. Though DIBAs initially seemed to be promising antiviral candidates, there were clinical issues with their stability. DIBAs tend to cyclize into benzisothiazolones which do not have the same potency when used to combat retroviruses as the original compound. Additionally, glutathione can reduce the disulfide bonds in DIBA thereby restricting its function in vitro. Mercaptobenzamides Mercaptobenzamide prodrugs transfer acyl group to 36th cysteine residue of NCp7 and the acyl group then migrates to neighboring lysine residue that triggers the ejection of Zn. The mercaptobenzamide and its corresponding prodrug yielded additivity to synergy when combined with known HIV drugs. Moreover