The study investigates the assembly of fluorescent parvovirus-like particles (VLPs) by fusing canine parvovirus (CPV) VP2 protein to the C-terminus of enhanced green fluorescent protein (EGFP). The non-truncated EGFP-VP2 and constructs with N-terminal deletions of VP2 (-14, -23, and -40 amino acids) were produced in insect cells, purified, and analyzed using fluorescence correlation spectroscopy (FCS), confocal microscopy, and electron microscopy. The results show that the non-truncated EGFP-VP2 and constructs with deletions of 23 and 40 amino acids formed VLPs with hydrodynamic radii of 17 nm, 20 nm, and 14 nm, respectively. However, the construct with a 14 amino acid deletion (-14) failed to form VLP-like structures. FCS measurements revealed that the number of fluorescent moieties per VLP was higher in the constructs with deletions of 23 and 40 amino acids compared to the non-truncated construct. The study demonstrates that FCS is a valuable tool for analyzing virus assembly and provides insights into the structural requirements for VLP formation.The study investigates the assembly of fluorescent parvovirus-like particles (VLPs) by fusing canine parvovirus (CPV) VP2 protein to the C-terminus of enhanced green fluorescent protein (EGFP). The non-truncated EGFP-VP2 and constructs with N-terminal deletions of VP2 (-14, -23, and -40 amino acids) were produced in insect cells, purified, and analyzed using fluorescence correlation spectroscopy (FCS), confocal microscopy, and electron microscopy. The results show that the non-truncated EGFP-VP2 and constructs with deletions of 23 and 40 amino acids formed VLPs with hydrodynamic radii of 17 nm, 20 nm, and 14 nm, respectively. However, the construct with a 14 amino acid deletion (-14) failed to form VLP-like structures. FCS measurements revealed that the number of fluorescent moieties per VLP was higher in the constructs with deletions of 23 and 40 amino acids compared to the non-truncated construct. The study demonstrates that FCS is a valuable tool for analyzing virus assembly and provides insights into the structural requirements for VLP formation.