| Isolated reports have indicated that peptides can interact with macromolecules in the absence of a classically defined receptor. For example, as early as 1977, Votano and co-workers (Votano, J. R.; Gorecki, M.; and Rich, A. Science 1977, 81, 1216) had shown that selected small peptides (;The approach we have taken is one in which various proteins are digested with proteolytic enzymes in one compartment of a cell which is separated by a dialysis membrane (MWCO 3,500) from a second compartment containing the macromolecule. Small peptide fragments (MW ;We have applied this system to 9 different macromolecular sinks, using 3 different peptide generating proteins. The results of these studies, and the underlying hypothesis will be presented.;Based on what is known about peptide antibody interactions, we speculate that all of these peptide-macromolecule interactions may be part of a more general phenomena. In an attempt to evaluate the scope of such peptide-macromolecule interactions, a method has been developed for evaluating the affinity of large numbers of peptides (ca. 2,000) for various macromolecules. |
