Peptoid macrocycles: making the rounds with peptidomimetic oligomers.
Macrocyclic constraints are often employed to rigidify the conformation of flexible oligomeric systems. This approach has recently been used to organize the structure of peptoid oligomers, which are peptidomimetics composed of chemically diverse N-substituted glycine monomer units. In this review, we describe advances in the synthesis and characterization of cyclic peptoids. We evaluate how the installation of covalent constraints between the oligomer termini or side chains has been effective in defining peptoid conformations. We also discuss the potential applications for this promising family of macrocyclic peptidomimetics.
Yoo
Barney
B
Department of Chemistry, New York University, 100 Washington Square East, New York, NY 10003-6688, USA.
Shin
Sung Bin Y
SB
Huang
Mia Lace
ML
Kirshenbaum
Kent
K
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D005998:Glycine / Q000737:chemistry*; D047028:Macrocyclic Compounds / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D010456:Peptides, Cyclic / Q000138:chemical synthesis* / Q000737:chemistry; D034444:Peptoids / Q000737:chemistry*; D011487:Protein Conformation; D013237:Stereoisomerism
D047028:Macrocyclic Compounds; D010456:Peptides, Cyclic; D034444:Peptoids; D005998:Glycine