Peptoids, dynamic

Finally, dynamic peptoids, dynamic analogs of peptides and proteins, have been generated by polycondensation of complementary difunctional monomers derived... 

A peptoid pentamer of five poro-substituted (S)-N-(l-phenylethyl)glycine monomers, which exhibits the characteristic a-helix-like CD spectrum described above, was further analyzed by 2D-NMR [42]. Although this pentamer has a dynamic structure and adopts a family of conformations in methanol solution, 50-60% of the population exists as a right-handed helical conformer, containing all cis-amide bonds (in agreement with modeling studies [3]), with about three residues per turn and a pitch of 6 A. Minor families of conformational isomers arise from cis/trans-amide bond isomerization. Since many peptoid sequences with chiral aromatic side chains share similar CD characteristics with this helical pentamer, the type of CD spectrum described above can be considered to be indicative of the formation of this class of peptoid helix in general. 

Fafarman AT, Borbat PT, Freed JH, Kirshenbaum K. Characterizing the structure and dynamics of folded oligomers. Pulsed ESR smdies of peptoid heUces. Chem. Commun. 2007 377—379. 

R. Wills, A kinetic/dynamic perspective of a peptide and protein GRF and rHuIFN-alpha-2a in Peptides, Peptoids, and Proteins (Eds. P. Garzone, W. Colburn, M. Mokotoff), Harvey Whitney Books, Cincinnati, OH, 1991, pp. 117-127. 

Fig. 10 (a) Using molecular dynamics, protein-like peptoid sequences were obtained by iterative process of globule formation and addition/redistribution of polar residues on the globule surface, (b) Globule-to-coil transition was induced by titration with acetonitrile, which leads to unfolding of the globules, (c) The transition is more pronounced and sharper in the case of the protein-like sequence. Reproduced from [93], with permission from American Oiemical Society... 

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