The formation of well-ordered nanostructures by a process of self-association represents the essence of modern nanotechnology. Such self-assembled structures can be formed by a variety of building blocks, both organic and inorganic. Of the organic building blocks, peptides are among the most useful ones. The versatility of the peptides, in conjunction with their ability to form specific secondary structures, provides a unique platform for the design of nanomaterials with controllable structural features. Oligopeptides fold into secondary structures stabilized by multiple interactions that require the participation of both backbones and side chains, with the overwhelming majority being helical conformation with no cavity. While most cavities and pores are associated with the tertiary and quaternary structures of proteins, some helical oligopeptides are known to contains pores. For example the antibiotic oligopeptide gramicidin A folds into a ?-helix containing a 5? pore.
Design and Synthesis of Peptide Building Blocks for Tunable Biopolymers
Fenude Emma;Saviano Michele
2019
Abstract
The formation of well-ordered nanostructures by a process of self-association represents the essence of modern nanotechnology. Such self-assembled structures can be formed by a variety of building blocks, both organic and inorganic. Of the organic building blocks, peptides are among the most useful ones. The versatility of the peptides, in conjunction with their ability to form specific secondary structures, provides a unique platform for the design of nanomaterials with controllable structural features. Oligopeptides fold into secondary structures stabilized by multiple interactions that require the participation of both backbones and side chains, with the overwhelming majority being helical conformation with no cavity. While most cavities and pores are associated with the tertiary and quaternary structures of proteins, some helical oligopeptides are known to contains pores. For example the antibiotic oligopeptide gramicidin A folds into a ?-helix containing a 5? pore.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.