Here no significant effect from LRCM and PRCM on DNA mobility showed that these particles do not have an active role to play in DNA interaction and melittin is the only component in Polybee and Lipobee to participate in interaction with DNA duplex. Proteins are major constituents of blood serum and counter the load vehicle and pharma coactive agents while delivering through systemic circulations. Any obstruction in normal behavior of such blood serum proteins might lead to harmful consequences to the subject. As a model system of study, we chose fetal bovine serum to establish effects of free melittin and its nanoform mulations, Lipobee and Polybee so normal spectroscopic properties. UV absorbance study was performed on 50��M melittin incubated 10% FBS solution. No bathochromic shift in UV absorbance pattern was noted from FBS solution but absorbance was increased after incubation with free melittin. A decrease in absorbance was seen in case of Lipobee, which reached a level similar to nontreated FBS when compared to Polybee. This observation could be explained due to the additional absorbance from added for mulations, signifying no specific interaction of melittin in free or nanoform mulation form with serum proteins. The fate of released melittin can be rationalized in regards to its interaction with genomic pool cellular components. One among them could have resulted from an interaction of melittin with DNA. To explore the interactions of melittin with DNA in-silico, we performed docking studies of melittin into double stranded DNA. It has been found that melittin intertwines well and remains within a close Nutlin-3b proximity of DNA structures, forming 17H-bondinteractions and 3hydrophobicinteractions with phosphate groups and base pairings of DNA. It has also been noticed that nitrogen and oxygen in both backbones and side chains formed an H bond only with oxygen of phosphate groups, not with nitrogen and oxygen in paired bases. However, these strong H-bond interactions changed the conformations of paired bases, making the H-bond Piperacillin Sodium distance between paired bases mostly enlarged.