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n→π* interactions in poly(lactic acid) suggest a role in protein folding
Robert W Newberry1, Ronald T Raines
1Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706-1322, USA.
Abstract:
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→π* interactions between sequential ester carbonyl groups contribute 0.44 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.
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