Aza-proline effectively mimics l-proline stereochemistry in triple helical collagen.

摘要: The prevalence of L-amino acids in biomolecules has been shown to have teleological importance biomolecular structure and self-assembly. Recently, biophysical studies demonstrated that natural can be replaced with non-natural achiral aza-amino folded protein structures such as triple helical collagen. However, the structural consequences acid incorporation not elucidated context any relevant biomolecule. Herein, we use X-ray crystallography provide first atomic resolution crystal an residue embedded within a structure, definitively illustrating aza-proline capacity effectively mimic stereochemistry amino We further corroborate this finding density functional theory computational analysis showing for is energetically favored when arranged aza-proline-hydroxyproline-glycine motif. In addition providing fundamental insight into peptide stereochemical mimics could far reaching impacts areas ranging from synthetic materials drug design.