Foldamers

From Wikipedia, the free encyclopedia

Crystal structure of a foldmer reported by Lehn and coworkers in Helv. Chim. Acta., 2003, 86, 1598-1624.
Crystal structure of a foldmer reported by Lehn and coworkers in Helv. Chim. Acta., 2003, 86, 1598-1624.

A foldamer is a discrete chain molecule or oligomer that adopts a secondary structure stabilized by non-covalent interactions [1] [2]. They are artificial molecules that mimic the ability of proteins, nucleic acids, and polysaccharides to fold into well-defined conformations, such as helices and β-sheets. Foldamers have been demonstrated to display a number of interesting supramolecular properties including molecular self-assembly, molecular recognition, and host-guest chemistry. They are studied as models of biological molecules and have been shown to display antimicrobial activity. They also have great potential application to the development of new functional materials.

Examples:

  • m-Phenylene ethynylene oligomers are driven to fold into a helical conformation by solvophobic forces and aromatic stacking interactions.
  • β-peptides are composed of amino acids containing an additional methylene unit between the amine and carboxylic acid. They are more stable to enzymatic degradation and have been demonstrated to have antimicrobial activity.
  • Aedamers that fold in aqueous solutions driven by hydrophobic and aromatic stacking interactions.

[edit] References

Important Reviews:

  1. ^  Gellman, S.H. (1998). "Foldamers: a manifesto". Acc. Chem. Res 31 (4): 173–180. doi:10.1021/ar960298r. 
  2. ^  Hill DJ, Mio MJ, Prince RB, Hughes TS, Moore JS (2001). "A field guide to foldamers". Chem. Rev. 101 (12): 3893–4012. doi:10.1021/cr990120t. PMID 11740924. 

[edit] Further reading

[edit] External links