Antibodies Against Synthetic Peptides

Abstract

The introduction of a simple and efficient peptide synthesis methodology in the early 1960’s (1) put a powerful research tool at the disposal of biologists and protein chemists alike. Thus, it was immediately feasible to synthesize not only biologically active peptides, but also discrete segments of proteins. It was obvious from the start, also, that this technology could be coupled with longstanding immunologic procedures whereby small molecules can be used as antigenic materials (2). Indeed, the approach was soon applied to a number of proteins in a quest to find what features made them antigenic (3). It is fair to say, though, that the full capacity of the combined immunologic and synthetic techniques was never exploited during the 1960’s and 1970’s. Since then advances in the field of DNA sequencing have provided a plethora of sequence information about proteins, real and putative, many of which have never been isolated, never mind characterized. The sequence data can be utilized in a variety of ways, especially in conjunction with computer-aided predictive schemes that allow a degree of meaningful conjecture about the three-dimensional structure of a given sequence. Among the ends to which DNA/protein sequence data can be put is the chemical synthesis of peptides corresponding to portions of the protein.