A supramolecular method to control protein assembly using a biogenic polyamine

ABSTRACT

We report a method to modulate the formation and stability of nano- and micro-assemblies of bovine serum albumin (BSA) formed with CB[7] using the treatment of a biogenic polyamine such as spermine (SPM). Our findings show that SPM impacts the size and surface charge of BSA-CB[7] assemblies, effectively reducing the size of nanoscale particles and making their surface charges more positive. Conversely, for larger particles spanning more than a few micrometres in diameter, SPM treatment is less effective in reducing their size. This ineffectiveness is attributed to the interaction between the external surface of CB[7] and BSA, which remains relatively unaffected by SPM. Over time, with an excess of CB[7], this interaction becomes more pronounced, resulting in aggregation of large particles and subsequent sedimentation. Since SPM is a biogenic polyamine found at elevated levels in cancerous tissues, this result may offer a strategic direction for designing supramolecular systems to control protein assemblies in oncological environments, highlighting the significant potential of supramolecular chemistry in biomedical applications.

GRAPHICAL ABSTRACT

KEYWORDS:

• Protein assembly
• cucurbituril
• bovine serum albumin
• spermine
• biogenic amine

Acknowledgments

This work was supported by the grant of Research Institute of Medical Science, Daegu Catholic University (2023).

Disclosure statement

No potential conflict of interest was reported by the author(s).