Serum albumin could potentially be exploited to form a protein corona on gold nanorods (AuNRs) for drug delivery because of its endogenous functionality as a small molecule carrier. However, the cetyltrimethylammonium bromide (CTAB) surfactant, which is a synthesis byproduct passivating AuNRs to confer colloidal stability, could also cause its conformational change upon interaction with serum albumin during the process of corona formation, thus altering its biological functions. Unfortunately, a clear understanding of how exactly human serum albumin (HSA) would change its conformation as it interacts with AuNR-CTAB is presently lacking. Here, we made use of coarse-grain molecular dynamics (CGMD) simulation to elucidate the interaction between HSA and AuNR-CTAB leading to its widely reported conformational change. We showed that HSA could sequester CTAB from the surface of AuNRs and form HSA-CTAB complexes, which could also interact with other adjacent complexes through "cross-linking" by the clusters of CTAB. Such a HSA-CTAB complex resulted in the observed conformational change of HSA, which we verified empirically with an esterase activity assay and by analyzing the root-mean-square-deviation of the HSA molecules from CGMD. The conformational change of HSA was not observed in AuNRs passivated with other negatively or positively charged surface ligands such as polystyrene sulfonate and polydiallyldimethylammonium chloride. Therefore, our study revealed that the conformational change experienced by HSA may not necessarily be attributed to protein unfolding on the surface of the AuNR due to charge interactions but rather to the instability of the surface ligands on the AuNRs which allows them to be sequestered by HSA to form HSA-CTAB complexes.