Badhe Ravindra V, Kumar Pradeep, Choonara Yahya E, Marimuthu Thashree, du Toit Lisa C, Bijukumar Divya, Chejara Dharmesh R, Mabrouk Mostafa, Pillay Viness
Wits Advanced Drug Delivery Platform Research Unit, Department of Pharmacy and Pharmacology, School of Therapeutic Sciences, Faculty of Health Sciences, University of the Witwatersrand, Johannesburg, 7 York Road, Parktown 2193, South Africa.
Department of Refractories, Ceramics and Building Materials, National Research Centre, 33 El-Bohouth St. (former El-Tahrir St.), Dokki, Giza P.O. 12622, Egypt.
Materials (Basel). 2018 Apr 16;11(4):609. doi: 10.3390/ma11040609.
Stigmergy, a form of self-organization, was employed here to engineer a self-organizing peptide capable of forming a nano- or micro-structure and that can potentially be used in various drug delivery and biomedical applications. These self-assembling peptides exhibit several desirable qualities for drug delivery, tissue engineering, cosmetics, antibiotics, food science, and biomedical surface engineering. In this study, peptide biomaterial synthesis was carried out using an environment-reliant auto-programmer stigmergic approach. A model protein, α-gliadin (31, 36, and 38 kD), was forced to attain a primary structure with free –SH groups and broken down enzymatically into smaller fragments using chymotrypsin. This breakdown was carried out at different environment conditions (37 and 50 °C), and the fragments were allowed to self-organize at these temperatures. The new peptides so formed diverged according to the environmental conditions. Interestingly, two peptides (with molecular weights of 13.8 and 11.8 kD) were isolated when the reaction temperature was maintained at 50 °C, while four peptides with molecular weights of 54, 51, 13.8, and 12.8 kD were obtained when the reaction was conducted at 37 °C. Thus, at a higher temperature (50 °C), the peptides formed, compared to the original protein, had lower molecular weights, whereas, at a lower temperature (37 °C), two peptides had higher molecular weights and two had lower molecular weights.
自催化作用，一种自组织形式，在此被用于设计一种能够形成纳米或微结构的自组织肽，这种肽有可能用于各种药物递送和生物医学应用。这些自组装肽在药物递送、组织工程、化妆品、抗生素、食品科学和生物医学表面工程方面展现出几种理想的特性。在本研究中，肽生物材料的合成是采用一种依赖环境的自动编程自催化方法进行的。一种模型蛋白，α-麦醇溶蛋白（31、36和38千道尔顿），被迫获得具有游离-SH基团的一级结构，并使用胰凝乳蛋白酶将其酶解成更小的片段。这种酶解在不同的环境条件（37和50℃）下进行，并且让这些片段在这些温度下自组织。如此形成的新肽根据环境条件而有所不同。有趣的是，当反应温度保持在50℃时，分离出了两种肽（分子量分别为13.8和11.8千道尔顿），而当反应在37℃进行时，获得了四种分子量分别为54、51、13.8和12.8千道尔顿的肽。因此，在较高温度（50℃）下形成的肽与原始蛋白质相比分子量较低，而在较低温度（37℃）下，两种肽分子量较高，两种肽分子量较低。
