Design and construction of biologically active peptides, including enzymes
Amphiphilic secondary structural regions have been found to be of great importance to the biological and physical properties of a variety of peptides and proteins that act at membrane surfaces. For systems ranging from apolipoproteins through toxins to peptide hormones we have prepared peptide models that have minimal homology to the corre— sponding regions of the natural peptides and proteins but simulate their biological and physical behavior. Most of our peptides have been synthe— sized by the stepwise solid phase method. However, in the synthesis of two of our models for apolipoprotein A—I we have utilized an oxime polymer that we have developed for a fragment synthesis—condensation approach. The latter approach will probably find considerable applica— tion, particularly in the preparation of large peptide and protein models.