ABSTRACT
Peptides of natural or synthetic origin are compounds involved in a variety of biological functions. Solid-phase peptide synthesis consists of three distinct sets of operations: chain assembly on a resin; simultaneous or sequential cleavage, and deprotection of the resin-bound, fully protected chain; and purification and characterization of the target peptide. The esterification of the first amino acid to the hydroxyl group on the resin is one of the key steps to producing a high quality peptide. The peptide quality is examined routinely by the analytical High Performance Liquid Cromatografy to determine the purity in conjunction with mass spectral analysis to determine the identity. Peptide modification with a chelating agent gives the very important opportunity to prepare stable metallo-peptides. Conformational analysis of linear peptides is considerably more difficult than that of cyclic peptides because of the absence of the cyclization constraints.
