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1.D.80.  The Fluorinated Sugar-Tripeptide (FSTP) Family 

Acyclic αγα-tripeptides derived from fluorinated-furanoid sugar amino acid frameworks act as reverse-turn inducers with a U-shaped conformation, whereas the corresponding nonfluorinated αγα-tripeptides show random peptide conformations (Burade et al. 2017). NMR studies showed that the presence of bifurcated weak intramolecular hydrogen bonding (F···HN) and N+···Fδ- charge-dipole attraction compel the amide carbonyl groups to orient antiperiplanar to the C-F bond, thus, demonstrating the role of the fluorine substituent in stabilizing the U-shaped conformation.  A pentameric self-assembly has been demonstrated, and these show fibers that form nanorods. The antiparallel self-assembled pore of the fluorinated tripeptides promote selective anion-transport activity.The order of anion selectivity was:  SCN- > Cl- > NO3- > AcO- > F- (Burade et al. 2017).

References associated with 1.D.80 family:

Burade, S.S., S.V. Shinde, N. Bhuma, N. Kumbhar, A. Kotmale, P.R. Rajamohanan, R.G. Gonnade, P. Talukdar, and D.D. Dhavale. (2017). Acyclic αγα-Tripeptides with Fluorinated- and Nonfluorinated-Furanoid Sugar Framework: Importance of Fluoro Substituent in Reverse-Turn Induced Self-Assembly and Transmembrane Ion-Transport Activity. J Org Chem. [Epub: Ahead of Print] 28485150