Kinetics of albumin microbubble dissolution in aqueous media
Aaqib H Khan1, Sameer V Dalvi1
1Chemical Engineering, Indian Institute of Technology Gandhinagar, Palaj, Gandhinagar 382355, Gujarat, India. sameervd@iitgn.ac.in.
This study investigates the dissolution behavior of protein microbubbles, revealing how shell parameters like interfacial tension and resistance change during dissolution. Understanding these protein microbubble dynamics is crucial for their use in medical imaging and drug delivery.
Area of Science:
- Biomaterials Science
- Chemical Engineering
- Acoustic Medicine
Background:
- Microbubbles are vital as ultrasound contrast agents and drug delivery vehicles, requiring stable persistence in blood.
- Existing research extensively covers lipid microbubble dissolution, but lacks data on protein microbubble kinetics and shell properties.
- Characterizing protein microbubble shell parameters is essential for optimizing their biomedical applications.
Purpose of the Study:
- To investigate the dissolution behavior and kinetics of protein microbubbles.
- To estimate key shell parameters (interfacial tension, shell resistance, elasticity) for protein microbubbles.
- To evaluate the influence of processing conditions on these protein shell parameters.
Main Methods:
- Synthesized protein microbubbles using bovine serum albumin (BSA) via sonication.
- Monitored microbubble dissolution kinetics (radius vs. time) numerically.
- Applied a mass transfer model to estimate shell parameters from dissolution data.
Main Results:
- Observed protein shell disengagement from the gas-liquid interface during dissolution, leading to sudden microbubble disappearance.
- Quantified drastic increases in interfacial tension and significant reductions in shell resistance as protein molecules desorbed.
- Evaluated the impact of preheating temperature, microbubble size, and composition on shell parameters.
Conclusions:
- Protein microbubble dissolution is characterized by shell detachment and rapid disappearance.
- Shell parameters dynamically change during dissolution, offering insights into protein shell stability.
- This research provides critical data for designing and utilizing protein microbubbles in biomedical applications.
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