Accession Number:

ADA525010

Title:

Innovative Foldamers: Engineering Heterochiral Peptides

Descriptive Note:

Corporate Author:

NAVAL RESEARCH LAB WASHINGTON DC CHEMISTRY DIV

Personal Author(s):

Report Date:

2009-01-01

Pagination or Media Count:

3.0

Abstract:

Innovative Foldamers The field of foldamer design promises new routes to important compounds for use in sensors, smart materials, and catalysts. The term foldamer refers to a molecule that folds into a structurally stable state in solution. Proteins and peptides are an important class of natural foldamers that carry out a host of essential functions in biology, including molecular recognition, information storage, catalysis, and controlled crystallization of inorganic materials. The desire to mimic such functions with synthetic molecules inspires the field of foldamer design. Of the foldamers under development, beta-helices -- peptide helices containing amino acids with alternating chirality -- represent an intriguing and relatively unexplored subclass of peptide-based foldamers. Very few beta-helical peptides exist in nature, and all of these compounds adopt their active beta-helical structures in hydrophobic membrane environments. However, for many potential biomimetic or bioinspired applications, water or other polar solvents will likely be the medium of choice. In our research, therefore, we pose the question Can engineered beta-helices discretely fold in polar media such as methanol, and ultimately water

Subject Categories:

  • Biochemistry
  • Atomic and Molecular Physics and Spectroscopy
  • Bionics

Distribution Statement:

APPROVED FOR PUBLIC RELEASE