Despite the worldwide attention garnered by AIDS, the HIV therapies of today do not extend to a wide variety of viral targets. The HIV-1 capsid structure bears significance as a drug target via its protective properties for the overall maturation of the virion. Individual capsid dimer units combine to form an electron dense, protective core around the RNA strands via proteolytic cleavage of the capsid protein (p24) from the Gag polyprotein complex. A hydrophobic pocket is created prior to final beta-hairpin/helix formation of the initial 13 Nterminal residues of the capsid protein. Amino acid residue sequence alignment studies of the protein (p24) show the N-terminal Proline and residue 51 (Aspartate) to be highly conserved. These two residues form a salt-bridge that stabilizes the final formation of the protein. The UNIX-based program DOCK 4.0 was used to screen more than 400,000 compounds in search of ligands and pharmacophores capable of interacting with key N-terminal pocket residues. Numerous lead compounds have been analyzed which have notable potential for inhibiting capsid formation and subsequent retardation of HIV maturation.