Structure of Porous Columns Self-assembled from Dendritic Dipeptides

Synthetic pores are an important step in the development of biomimetic materials incorporating features such as trans-membrane channels, gene delivery, protein folding, and selective encapsulation. We have used small-angle xray scattering to study helical pores self-assembled from dendritic dipeptides. The main features of the supramolecular assembly are computed by least-squares fitting the parameters of a simplified structural model to the x-ray diffraction data. This work reports the supramolecular assembly temperature stability and conformational changes of the 3-dimensional packing as a function of dipeptide structure and stereochemistry. The results provide a methodology to design the synthetic pores in order to control the pore size and separation at the \AA\, level, according to the desired function.