Early events in aggregation of proteins are not easily accessible by experiments. In this work, we perform a 5-ns
molecular dynamics simulation of an ensemble of 27 copies of b2-microglobulin in explicit solvent. During the simulation, the
formation of intermolecular contacts is observed. The simulation highlights the importance of apical residues and, in particular, of
those at the N-terminus end of the molecule. The most frequently found pattern of interaction involves a head-to-head contact
arrangement of molecules. Hydrophobic contacts appear to be important for the establishment of long-lived (on the simulation
timescale) contacts. Although early events on the pathway to aggregation and fibril formation are not directly related to the endstate
of the process, which is reached on a much longer timescale, simulation results are consistent with experimental data and in
general with a parallel arrangement of intermolecular b-strand pairs.
