Thermal unfolding of water-soluble peptoid oligomer secondary structure

ORGN 771

Justin M. Holub, jmh456@nyu.edu and Kent Kirshenbaum, kent@nyu.edu. Department of Chemistry, New York University, 100 Washington Square East, New York, NY 10003
We describe the synthesis and characterization of water-soluble peptoid oligomers incorporating N-(S)-methoxypropyl-glycine monomer units. Peptoid sequences of varying chain length were subjected to elevated temperatures and the structural consequences were evaluated by circular dichroism spectroscopy. Our findings indicate that the polyproline I-type helical structure can be essentially abolished by thermal denaturation. Interestingly, the reversible unfolding process was observed to be highly cooperative in longer oligomers (>13mers), but not at shorter chain lengths.