Ligand-Mediated Mechanical Enhancement in Protein Complexes at Nano- and Macro-Scale
Ligand-Mediated Mechanical Enhancement in Protein Complexes at Nano- and Macro-Scale
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DOI：
10.1021/acsami.3c14653
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发表时间：
2023-12-19
影响因子：
9.5
通讯作者：
Kim，Minkyu
中科院分区：
文献类型：
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作者：
Kim，Samuel;Cathey，Marcus V. J.;Kim，Minkyu
蛋白质自组装在生物功能和生物材料的构建中起着至关重要的作用。虽然这些组装体的物理结合提供了高特异性，但这种优势往往会损害蛋白质复合物的整体耐久性。为了应对这一挑战，我们提出了一种新的策略，加强分子自组装的蛋白质复合物介导的配体。已知其强大的非共价相互作用与生物素，链霉亲和素（SAV）四聚体进行检查，以了解配体如何影响蛋白质复合物的机械强度在纳米级和宏观尺度，采用原子力显微镜为基础的单分子力光谱，流变学和生物侵蚀分析。我们的研究表明，生物素结合增强了单个SAv四聚体在纳米级的机械强度。当SAv四聚体用作水凝胶内的交联点时，这种增强转化为改善的剪切弹性和降低的生物侵蚀速率。这种方法在不影响特异性的情况下增强了蛋白质基材料的机械强度，有望为先进的生物技术应用开辟新的途径，包括自组装、稳健的仿生支架和软机器人。
Protein self-assembly plays a vital role in a myriad of biological functions and in the construction of biomaterials. Although the physical association underlying these assemblies offers high specificity, the advantage often compromises the overall durability of protein complexes. To address this challenge, we propose a novel strategy that reinforces the molecular self-assembly of protein complexes mediated by their ligand. Known for their robust noncovalent interactions with biotin, streptavidin (SAv) tetramers are examined to understand how the ligand influences the mechanical strength of protein complexes at the nanoscale and macroscale, employing atomic force microscopy-based single-molecule force spectroscopy, rheology, and bioerosion analysis. Our study reveals that biotin binding enhances the mechanical strength of individual SAv tetramers at the nanoscale. This enhancement translates into improved shear elasticity and reduced bioerosion rates when SAv tetramers are utilized as cross-linking junctions within hydrogel. This approach, which enhances the mechanical strength of protein-based materials without compromising specificity, is expected to open new avenues for advanced biotechnological applications, including self-assembled, robust biomimetic scaffolds and soft robotics.