Structure-function relationships in peptoids: recent advances toward deciphering the structural requirements for biological function

• Published in: Organic & biomolecular chemistry Vol. 7; no. 8; pp. 1508 - 1524
• Main Authors: Fowler, Sarah A, Blackwell, Helen E
• Format: Journal Article
• Language: English
• Published: England 01.01.2009
• Subjects: Amino Acid Sequence; Amyloid - chemistry; Anti-Infective Agents - chemistry; Biomimetics; Glycine - chemical synthesis; Glycine - chemistry; Glycine - metabolism; Islet Amyloid Polypeptide; Molecular Sequence Data; Peptoids - chemical synthesis; Peptoids - chemistry; Peptoids - metabolism; Protein Binding; Protein Conformation; Protein Folding; Pulmonary Surfactants - chemistry; Structure-Activity Relationship
• ISSN: 1477-0520; 1477-0539
• DOI: 10.1039/b817980h

Oligomers of N-substituted glycine, or peptoids, are versatile tools to probe biological processes and hold promise as therapeutic agents. An underlying theme in the majority of recent peptoid research is the connection between peptoid function and peptoid structure. For certain applications, well-folded peptoids are essential for activity, while unstructured peptoids appear to suffice, or even are superior, for other applications. Currently, these structure-function connections are largely made after the design, synthesis, and characterization process. However, as guidelines for peptoid folding are elucidated and the known biological activities are expanded, we anticipate these connections will provide a pathway toward the de novo design of functional peptoids. In this perspective, we review several of the peptoid structure-function relationships that have been delineated over the past five years.