Foldamer

In chemistry, a foldamer is a discrete chain molecule (oligomer) that folds into a conformationally ordered state in solution.

They are artificial molecules that mimic the ability of proteins, nucleic acids, and polysaccharides to fold into well-defined conformations, such as α-helices and β-sheets.

This type of analysis may be applied to small proteins as well; however, as of 2024, computational technology is unable to simulate all but the shortest of sequences.

[6] The folding pathway of a foldamer can be determined by measuring the variation from the experimentally-determined favored structure under different thermodynamic and kinetic conditions.

Changes in the temperature, solvent viscosity, pressure, pH, and salt concentration can all yield valuable information about the structure of the foldamer.

[6] Noncovalent intermolecular interactions, albeit individually small, collectively alter chemical reactions in major ways.

[8] The amino acids of these peptides only differ by one (β), two (γ), or three (δ) methylene carbons, yet the structural changes were profound.

Additionally, with multiple methylene carbons between the carboxyl and amino termini of the flanking peptide bonds, varying R-group side chains can be designed.