Fluorescence properties of N, N'-bis(salicylidene) trans 1, 2-diaminocyclohexane (H L) is used to probe the anionic (SDS), cationic (CTAB) and nonionic (TX-100) micelles as well as in serum albumins (BSA and HSA) and chicken egg white lysozyme (LYZ) by steady state and picosecond time-resolved fluorescence spectroscopy. The fluorescence band intensity was found to increase with concomitant blue-shift with gradual addition of different surfactants. All the experimental results suggest that the probe molecule resides in the micelle-water interface rather than going into the micellar core. However, the penetration is more towards the micellar hydrocarbon core in nonionic surfactant (TX-100) while comparing with ionic surfactants (SDS and CTAB). Several mean microscopic properties such as critical micelle concentration, polarity parameters and binding constant were calculated in presence of different surfactants. The decrease in nonradiative decay rate constants in micellar environments indicates restricted motion of the probe inside the micellar nanocages with increasing fluorescence emission intensity and quantum yields. Further in this work, we also investigated the interaction behavior of the probe with different proteins at low concentrations under physiological conditions (pH = 7.4). Stern-Volmer analysis of the tryptophan (Trp) fluorescence quenching data in presence of probe reveals Stern-Volmer constant (K) as well as bimolecular quenching rate constant (K). The binding constant as well as the number of binding sites of the probe with proteins were also monitored and found to be 1:1 stoichiometry ratio.