n→π~* interactions in poly(lactic acid) suggest a role in protein folding

摘要

Poly(lactic acid) (PLA) is a versatile synthetic polyester. We noted that this depsipeptide analog of polyalanine has a helical structure that resembles a polyproline II helix. Using natural bond orbital analysis, we find that n→n~* interactions between sequential ester carbonyl groups contribute 044 kcal mol~(- 1) per monomer to the conformational stability of PLA helices. We conclude that analogous n→π~* interactions could direct the folding of a polypeptide chain into a polyproline II helix prior to the formation of hydrogen bonds between backbone amides.