Hydrophobic effect is one of the major driving forces in biomolecular interactions. Biological molecules such as proteins and nucleic acids contain numerous hydrophobic components, and their interactions play critical roles in protein folding-unfolding and protein aggregation. In our study, we have carried out molecular dynamics simulation to understand the effect of caffeine on hydrophobic aggregation of di-t-butyl-methane (DTBM) molecules. For this we consider aqueous solutions of a regime of caffeine:DTBM stoichiometric ratios. From the calculations of site-site radial distribution functions followed by the coordination number analyses and spatial distribution plots we have observed the disruption of hydrophobic moieties of DTBM aggregates in 10:1 or more stoichiometric ratio of caffeine:DTBM systems. Calculations of binding affinities, preferential interaction parameters, and effect of caffeine cluster's size on aggregation show that though the binding affinity of DTBM with itself is more when compared to that of caffeine-DTBM, with increasing caffeine number the former decreases. On the other hand, in the presence of higher number of caffeine molecules the formation of caffeine clusters takes place and these caffeine clusters form a hydrophobic environment in which DTBM molecule is encapsulated. The presence of a significant number of water molecules in this confinement also ensures the hydration of DTBM. Moreover, these caffeine clusters also act as barriers and physically block the DTBM molecules to interact with the like molecules leading to a disruption of DTBM aggregates in caffeine solution.