The ILQINS hexapeptide is a self-assembling biological material of wide interest due to its biological relevance, rapid aggregation behaviour and unsual fibril morphologies. ILQINS was previously identified by the applicant and experimental collaborators as a very strongly amyloidogenic subsequence of the Hen’s Egg-White Lysozyme protein, a natural antibiotic commonly used as a food additive. The aggregation behaviour of ILQINS is of interest as potentially leading to a strong and versatile biomaterial which could be manufactured very cheaply from natural sources using existing technology and infrastructure. The project will leverage calculation methods and software which were developed and implemented in Luxembourg by Dr Berryman & Professor Schilling and which have already been proven in studies of other biological and soft-matter systems, to develop a phase diagram and kinetic scheme for ILQINS structure formation. The dependencies of the aggregation behaviour on temperature, pH and other experimentally accessible variables will be identified in order to create a self-assembling material which can be controlled in a systematic way. Other protein biomaterials (such as silk and keratin) have been part of human technology for millenia however the potential for innovation in this field based on an atomic-level understanding of the assembly process and of the finished product is still very large.