Date/Time: 04-05-2018 - Thursday - 05:00 PM - 07:00 PM
Alessandra Maria Bossi1

1, Dept. Biotechnology, University of Verona, Verona, , Italy

Biological functions in livings occurs by interactions, which ultimately imply stereo- and chemical-complementarity between the binding partners. In protein interaction, definite protein segments, such as exposed loops, helix-loop-helix motifs, etc. are involved in the formation of complexes that ultimately trigger the physiological responses.
Here, as a mimic of protein interactors, we attempted the synthesis of molecularly imprinted nanogels (nanoMIPs), performed by means of the molecular imprinting technique [1] and in precipitation polymerization conditions [2], that were addressed at the recognition of a structured peptide: the loop-shaped 9mer peptide with sequence C1-(X)n=7-C9 and fixed by a disulphyde bond.
The nanoMIPs were about 50 nm in size and 2 106 Da of mean molecular weight. They exhibited high affinity (Kd = 9 10-9 M) and structural selectivity for the loop-shaped peptide. Additionally, it was observed that the nanoMIPs promoted a fast formation of the loop-shaped peptide, by the oxidation of the linear precursor peptide [3].
These results demonstrated the feasibility of the structural imprinting and hinted at a possible role of the nanoMIPs to assist the refolding of peptide segments into defined structures, anticipating polymeric nanomachines for counteracting folding defects.

[1] G. Wulff and A. Sarhan, Angew. Chem. Int. Ed. 11, 341(1972); R. Arshady and K. Mosbach, Die Makromoleculare Chemie, 182, 687 (1981).
[2] N. Perez-Moral and A. G. Mayes, Anal. Chim. Acta 504, 15 (2004).
[3] L. Cenci, G. Guella, E. Andreetto, E. Ambrosi, A. Anesi, A.M. Bossi. Nanoscale 8, 15665 (2016).

Meeting Program

5:00 PM–7:00 PM Apr 5, 2018 (America - Denver)

PCC North, 300 Level, Exhibit Hall C-E