Additionally, PAMAM dendrimers have been reported to allow intermolecular tethering and utilized as cross-linking agents. It is likely that NP0 and NP5000 interact and transiently stabilize proteoglycans via electrostatic interactions due to their small size and ability to be taken into the tissue allowing GAG preservation. The possibility of such interactions was confirmed in the COL samples, where COL stimulation did not yield a similar pattern in GAG release upon NP addition, and no reduction in sGAGs was detected (Figure ). While COL has been reported to result in the loss of GAGs, interestingly, we observed a further increase in GAG release after the NP0 addition. Since the mechanism behind such interaction is not currently known, we hypothesize that the synergistic degradation effect may be driven by the disruption in the electrostatic forces that bind GAGs to collagen. Due to their size, highly cationic NP0 may drive a more significant disruption of the matrix structure, making it easier for COL to access collagen and cleave protein-GAG aggregates.