A Structuring Repeat for Peptide Design: Long Beta Ribbons

Abstract

Beta sheets are inherently length-limited; adding residues to the ends of model β-sheets does not necessarily grow the β-sheet. Here, we present a method for extending β-sheets to any length with a stabilizing repeat unit containing cross-strand Trp residues. Beta ribbons as long as 35 residues (approaching 100 Å in length) are reported and characterized.

Surface Self-Assembly of Dipeptides on Porous CaCO3 Particles Promoting Cell Internalization

“…Dipeptides and their derivatives as important building blocks can self-assemble into various architectures such as nanoparticles, vesicles, nanotubes, ribbons, and nanoflowers, playing a significant role in biomedical applications because of their excellent biocompatibility, bioadhesion, and biodegradability. − Meanwhile, dipeptides can be easily conjugated with additional functional groups (such as N-terminal fluorenyl-9-methoxycarbonyl, Fmoc) because of their abundant sequences, which further endows the dipeptides with a unique and controllable self-assembling behavior to form distinct morphologies and functions by modulating intermolecular interactions such as hydrogen bonds, electrostatic interactions, π–π stacking, hydrophobic forces, etc. , The mechanism of the self-assembling behavior of peptides in bulk medium has been intensively investigated by adjusting self-assembly conditions (pH value, temperature, ionic strength, etc.) and selecting peptide sequences, giving impressive and interesting results.…”