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Structure–function relationships in peptoids: Recent advances toward deciphering the structural requirements for biological function

Organic & Biomolecular Chemistry · 2009 · Vol. 7(8) · pp. 1508–1508
Sarah A. FowlerHelen E. Blackwell

Abstract

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.

Chemical Synthesis and AnalysisAntimicrobial Peptides and ActivitiesBiochemical and Structural CharacterizationPeptoidChemistryFolding (DSP implementation)Function (biology)Computational biologyStructure functionNanotechnologyBiochemistryBiologyPeptide

MeSH terms

Amino Acid SequenceAmyloidAnti-Infective AgentsGlycineMolecular Sequence DataProtein BindingProtein ConformationPulmonary SurfactantsStructure-Activity RelationshipProtein FoldingBiomimeticsPeptoidsIslet Amyloid Polypeptide
Citations
290
FWCI
10.76
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References
86
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99%
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Cited by
1,2,3‐Triazoles in Peptidomimetic Chemistry
European Journal of Organic Chemistry · 2011 · 277 citations
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