Brown R, Meldrum C, Cousins S
Department of Psychology, University of Newcastle, Callaghan, Australia.
Med Hypotheses. 1992 Aug;38(4):322-4. doi: 10.1016/0306-9877(92)90025-8.
The finding that codons for hydrophobic and hydrophilic amino acids are generally complemented by codons for hydrophilic and hydrophobic amino acids respectively has led to a novel observation. The antisense peptides coded for by the complementary DNA strand of biologically active peptides are able to bind their active sense counterparts with high specificity. Sense-antisense relationships have been observed in several peptide species as well as in receptor-ligand interactions. The idea that sense-antisense interactions are biologically relevant and indeed feasible among complex molecules prompts the examination of virus-host cell interactions. We propose such a sense-antisense interaction exists between the HIV glycoprotein gp120 and the intracellular domain of the HIV receptor CD4. This interaction is at a site which may be occupied by the proto oncogene product p56lck.
