Design of Short Linear Peptides That Show Hydrogen Bonding Constraints in Water

摘要

Short linear peptides with 4 to 10 residues are considered flexible molecules with entropic limitations on achieving unique conformations in water. Predominant conformation in these peptides can be achieved in water by incorporating amino acids that restrict access to conformational space, such as proline and aminoisobu-tyric acid (Aib) or by using noncovalent interactions, such as π-stacking. In the water environment, however, hydrogen bonds are generally not considered to be the major driving force for folding and constraining short linear peptides into a distinct conformation.