Abstract
Peptoids (N-substituted polyglycines and extended peptoids with variant backbone amino-acid monomer units) are oligomeric synthetic polymers that are becoming a valuable molecular tool in the biosciences. Of particular interest are their applications to the exploration of peptoid secondary structures and drug design. Major advantages of peptoids as research and pharmaceutical tools include the ease and economy of synthesis, highly variable backbone and side-chain chemistry possibilities. At the same time, peptoids have been demonstrated as highly active in biological systems while resistant to proteolytic decay. This review with 227 references considers the solid-phase synthetic aspects of peptoid preparation and utilization up to 2010 from the instigation, by R. N. Zuckermann et al., of peptoid chemistry in 1992.
Highlights
N-Substituted glycine oligomers (NSG), otherwise referred to as α-peptoids, are a readily accessible class of synthetic, non-natural peptide mimic of modular design into which a plethora of structuralMolecules 2010, 15 elements can be readily incorporated
It has been recently stated that the acylation and amination reactions at the core of NSG oligomer synthesis are not moisture sensitive [11], it had been previously observed that traces of water in anhydrous DMF or DMSO leads to n-1, n-2 NSG oligomers (i.e. N-terminal deletion sequences) due to N-terminal hydroxyl functions replacing the halogen through hydrolysis thereby terminating chain elongation [55]
A 50% [3] to 85-90% overall isolated yield for the 5-mer [10,52] has been stipulated as thresholds for amine submonomer use in NSG synthesis, so this set point is variable depending upon circumstances [64]
Summary
N-Substituted glycine oligomers (NSG), otherwise referred to as α-peptoids, are a readily accessible class of synthetic, non-natural peptide mimic of modular design into which a plethora of structural. Since the length has extended to 48-mers [6]; 50-mers for homo-oligomers with short linear side-chains; 60-mers via chemical ligation of 15-mers [7,8] and even 150-mers by bio-ligation using the cysteine protease, clostripain [9]. Protein-protein interactions are important in the cellular context and the study of these interfaces is needed for fundamental research in medicine and the bio-chemical sciences, protein capture and purification, diagnostics, etc. There is primary sequence alignment of carbonyl groups and side-chains between α-peptides and α-peptoids when countercurrent oligomer direction is correlated (Figure 3). NSG’s present a platform for the study of protein interactions beyond those approachable by small molecules defined by Lipinski’s rules and α-peptides
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