Influence of protein nativity on the stability of bovine serum albumin coated microbubbles

• DOI: 10.1016/j.isci.2024.109286
• Publication Date: 2024-02-21T09:17:41Z
• Authors: Palash Dhara; Niyati Shah; Vidya Sundaram; Ashutosh Srivastava; Alexander A. Solovev; Yongfeng Mei; Dmitry A. Gorin; Krishna Kanti Dey
• Keywords: Bovine serum albumin; Biocompatibility; Serum Albumin

Protein-coated microbubbles have become one of the emerging platforms in biomedical research as theranostic agents. In recent years, been extensively used ultrasound contrast agents and carriers molecular cargoes, pertaining to which several studies focused on tuning properties these bubbles achieve a higher degree biocompatibility extended stability. Synthesis has so far traditionally carried out with pre-heated proteins like bovine serum albumin (BSA) shell coatings, owing ease making BSA crosslinked structures through disulfide bridge formation. We, however, performed experiments demonstrate that air core formed native are more stable compared those using denatured BSA. The experimental observations supported analytical modeling computational studies, offer insights into effect conformation stabilizing shells prolonging their lifetimes.