“…The complex formation from electrostatic interaction between negatively charged amino acids of GFP and positively charged amino acids of Tat or V was expected. Since the reduction in particle sizes from the dense and homogeneous arrangement between molecules during the complex formation has been reported (Saether et al, 2008;Gorajana et al, 2010), then the reduction of hydrodynamic particle sizes of the mixtures in comparing with the single protein or peptides indicated the interaction between GFP and peptides. Particle sizes of GFP, Tat, and V, as determined by dynamic light scattering (DLS), were 421.50 ± 83.79, 272.60 ± 61.38, and 451.80 ± 78.76 nm, respectively, whereas the particle sizes of Tat-GFP (1:1 molar ratio), V-GFP (1:1 molar ratio), and V-Tat-GFP (1:1:1 molar ratio) were reduced to 192.60 ± 41.13, 140.00 ± 8.71, and 226.00 ± 50.72 nm, respectively.…”