μCroTrap aims to mimic severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) by self-assembly of peptide fragments of the receptor-binding motif (RBM) of the spike protein (S-protein), present at the surface of the virus. Peptide sequences inspired by RBM will contain patches of residues involved in the Angiotensin-converting-enzyme 2 (ACE2) receptor binding. Sequences will be rationally engineered to be amphiphilic with the aim to drive their assembly into higher order spherical aggregates, resembling the supramolecular architecture of SARS-CoV-2. These supramolecular virus-mimetics will be screened by phage display for the discovery of peptide binders with adaptive conformation towards the supramolecular architecture and high affinity for the minimalistic RBM binding sequence. The antiviral potential of the lead peptides will be analyzed computationally. These sequences will be further engineered to form fibrous nanostructures upon binding to the S protein, leading to virus entrapment by gelation in-situ, thus inhibiting binding of SARS-CoV-2 to the receptors of host cells.