In the present study, we demonstrated that HOCl-modified serum albumins can bind to LAV gp120, and that HOCl-modified serum albumins possess the ability to efficiently neutralize entry of the NL4-3 laboratory strain. Since the 5'-half of NL4-3 was constructed from NY5 and the 3'-half from LAV the NL4-3 external envelope is iden-tical to the commercial LAV gp120 used in our SPR binding studies.