Peptoids that are helical and partially water soluble have been shown to self-assemble into microspheres when the peptoid solution is dried on a silicon substrate. Such microsphere coatings have great potential for use in biosensor technologies, specifically to increase the surface area for binding. However, in order to be useful, the peptoids must consistently form uniform coatings. In this study we investigated the effects of various coating protocol parameters on the uniformity of the resulting peptoid microsphere coatings, including (i) solvent, (ii) administration technique, and (iii) drying environment. In addition, we investigated the robustness of the coatings as well as the potential for using a glass substrate. These studies show that uniform, robust peptoid microsphere coatings can be formed using protic solvents, a full coverage administration technique, and drying in open air on silicon or glass substrates.
References
[1]
Zuckermann, R.N.; Kerr, J.M.; Kent, S.B.; Moos, W.H. Efficient method for the preparation of peptoids [oligo-(N-subsituted glycines)] by submonomer solid-phase synthesis. J. Am. Chem. Soc. 1992, 114, 10646–10647, doi:10.1021/ja00052a076.
Chen, X.; Ding, K.; Ayres, N. Investigation into fiber formation in N-alkyl urea peptoid oligomers and the synthesis of a water-soluble PEG/N-alkyl urea peptoid oligomer conjugate. Polym. Chem. 2011, 2, 2635–2642.
[12]
Sanii, B.; Kudirka, R.; Cho, A.; Venkateswaran, N.; Olivier, G.K.; Olson, A.M.; Tran, H.; Harada, R.M.; Tan, L.; Zuckermann, R.N. Shaken, not stirred: collapsing a peptoid monolayer to produce free-floating, stable nanosheets. J. Am. Chem. Soc. 2011, 133, 20808–20815, doi:10.1021/ja206199d.
[13]
Hebert, M.L.; Shah, D.; Blake, P.; Turner, J.P.; Servoss, S.L. Tunable peptoid microspheres: Effects of side chain chemistry and sequence. Org. Biomol. Chem. 2013, doi:10.1039/C3OB40561C.
[14]
De Santis, E.; Hjelmgaard, T.; Caumes, C.; Faure, S.; Alexander, B.D.; Holder, S.J.; Siligardi, G.; Taillefumier, C.; Edwards, A.A. Effect of capping groups at the N- and C-termini on the conformational preference of alpha, beta-peptoids. Org. Biomol. Chem. 2012, 10, 1108–1122.
