Ultrasonic synthesis of stable, functional lysozyme microbubbles
Ultrasonic synthesis of stable, functional lysozyme microbubbles
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DOI：
10.1021/la801093q
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发表时间：
2008-09-16
期刊：
影响因子：
3.9
通讯作者：
Caruso, Frank
中科院分区：
文献类型：
--
作者：
Cavalieri, Francesca;Ashokkumar, Muthupandian;Caruso, Frank
高强度超声诱导水介质中蛋白质分子的乳化和交联。稳定性和由此产生的蛋白质包被微泡的功能在许多应用中是至关重要的。例如，载药微泡在体内的稳定性应该足够长，这样它们只能在特定部位破裂以释放药物。在这项研究中，我们报道了在水溶液中使用高强度超声合成稳定和功能的微泡，包被化学还原的溶菌酶。在没有化学还原的情况下，天然溶菌酶不能产生稳定的微泡，这表明游离-SH官能团对蛋白质交联的重要性。通过控制分子内二硫键的化学还原程度和超声时间来控制溶菌酶分子间的交联程度。溶菌酶包被的微泡在几个月内保持稳定，并保持溶菌酶的酶（抗菌）活性。聚电解质一层一层（LbL）沉积在蛋白质壳空气核模板上，已被用作修饰微泡表面特性的通用方法，表明在这些微泡表面吸附潜在药物和/或生物标记物的可能性，可用于治疗和诊断应用。
High-intensity ultrasound induces emulsification and cross-linking of protein molecules in aqueous medium. The stability and the functionality of the resultant protein-coated microbubbles are crucial in many of their applications. For example, the stability of drug-loaded microbubbles should be sufficiently long enough, in vivo, so that they can be ruptured only at specific sites for release of the drugs. In this study, we report the synthesis of stable and functional microbubbles, coated with chemically reduced lysozyme, using high-intensity ultrasound in aqueous solution. In the absence of chemical reduction, stable microbubbles were not produced with native lysozyme, indicating the importance of free -SH functional groups for protein cross-linking. The degree of cross-linking between lysozyme molecules was controlled by manipulating both the extent of chemical reduction of the intramolecular disulfide bonds and sonication time. The lysozyme-coated microbubbles are stable for several months and retain the enzymatic (antimicrobial) activity of lysozyme. The layer-by-layer (LbL) deposition of polyelectrolytes onto the protein-shell air-core template has been used as a versatile procedure to modify the surface properties of the microbubbles, indicating the possibility of adsorbing potential drugs and/orbiolabels on the surface of these microbubbles for therapeutic and diagnostic applications.