Combining Experimental and Simulation Techniques to Understand Morphology Control in Pentapeptide Nanostructures.

A controlled route toward biocompatible nanostructures has immense relevance for drug delivery and tissue engineering. We present an experimental-computational study identifying factors that govern the formation of well-defined aggregates by self-assembled pentapeptides, using single amino acid substitution. A subtle interplay between peptide rigidity/flexibility, hydrogen-bonding capacity, partitioning of aromatic side chains, and influence of dimerization determines the formation of ordered and disordered aggregate structures, and shifts the balance between the emergence of spherical or ill-defined morphologies.