The applications of AIE-dyes in bioimaging exploits their sensitivity to viscosity and the concentration of specific proteins. The classical example, Thioflavin T (ThT), binds to β-amyloid fibrils by interaction of its -NMe2 group perpendicularly aligned to the peptide assembly surface. The drawbacks arising from the weak photophysical response of ThT can be removed by proper substitution of the molecular skeleton, however the cationic nature limiting its efficient aggregation and compatibility to the hydrophobic protein pockets still needs to be worked out. The remedy for this problem is proposed in the present study. The series of the dyes, shown in Scheme 1, possess the two parts of fluorophore still separated by single bond allowing to conformational equlibrium to take place. The previous study devoted to their properties in solution, indicated that the efficient FQY control can be obtained by the proper substitution with even mildly donating (D) or accepting (A) substituents. It was proven that both the strength of the pushpull effect and its direction affects the emission, and the presence of the two different substituents in the fluorescent core can cover the whole range of the FQY values. Here, the strategy based on the topology switch for the AIE-ACQ control is developed. Fluorescence of nine dyes, including pairs of regioisomers, is compared for solution, aggregates and solid state and discussed with support of theoretical approach, in comparison to previously reported analog bearing strong electron-donor. Upon aggregation (THF/water), the absorption spectra of 1-9 show a significant decrease in absorbance and alterations in the shape of bands as the aggregation proceeds. In general, the position of absorption does not change much except for dyes with R=CF3 (hypsochromic shift) and compound 1 (broad and complicated spectrum), while the modulation of emission upon aggregation depends on the substituents.