发现大分子和了解水下粘附的相关机制对于研究水生生态系统中底栖动物的基本生态学和开发工业中的仿生粘附材料至关重要。这里,我们使用定量蛋白质组学来评估在模型污染海鞘中独特的粘附结构-stolon的发展过程中蛋白质表达的变化,西奥娜·罗布斯塔。我们发现了16种粘附蛋白候选物在茎中表达增加,海鞘粘附蛋白1(AAP1)特别富含粘附相关的信号肽,氨基酸,和功能域。蛋白质印迹和免疫定位分析证实了地幔中突出的AAP1信号,外衣,Stolon,和粘性脚印,表明该蛋白质的界面作用。表面涂层和原子力显微镜实验验证了AAP1对各种材料的附着力,可能是通过特定的静电和疏水氨基酸与各种底物的相互作用。此外,分子对接计算表明AAP1通过氢键和盐桥在VonWillebrand因子A型(VWFA)域之间交联的潜力,增强其粘附能力。总之,新发现的负责永久水下粘附的界面蛋白,随着阐明的粘附机制,有望为仿生粘合材料和防污策略的开发做出贡献。重要声明:发现大分子并研究其参与水下粘附的相关机制对于了解水生生态系统中底栖动物的基本生态学以及在各种行业中开发创新的仿生粘合材料至关重要。使用多学科分析方法,我们从模型海洋污垢海鞘中鉴定出一种界面蛋白-海鞘粘附蛋白1(AAP1),西奥娜·罗布斯塔。AAP1的界面功能是通过静电和疏水相互作用实现的,基于VonWillebrand因子A型(VWFA)结构域的交联可能会增强AAP1的界面粘附力。AAP1界面功能的识别和验证,结合粘附机制的阐明,为开发仿生粘合材料和制定有效的防污策略提供了有希望的目标。
Discovering macromolecules and understanding the associated mechanisms involved in underwater adhesion are essential for both studying the fundamental ecology of benthos in aquatic ecosystems and developing biomimetic adhesive materials in industries. Here, we employed quantitative proteomics to assess protein expression variations during the development of the distinct adhesive structure - stolon in the model fouling
ascidian, Ciona robusta. We found 16 adhesive protein candidates with increased expression in the stolon, with
ascidian adhesive protein 1 (AAP1) being particularly rich in adhesion-related signal peptides, amino acids, and functional domains. Western blot and immunolocalization analyses confirmed the prominent AAP1 signals in the mantle, tunic, stolon, and adhesive footprints, indicating the interfacial role of this protein. Surface coating and atomic force microscopy experiments verified AAP1\'s adhesion to diverse materials, likely through the specific electrostatic and hydrophobic amino acid interactions with various substrates. In addition, molecular docking calculations indicated the AAP1\'s potential for cross-linking via hydrogen bonds and salt bridges among Von Willebrand factor type A domains, enhancing its adhesion capability. Altogether, the newly discovered interfacial protein responsible for permanent underwater adhesion, along with the elucidated adhesion mechanisms, are expected to contribute to the development of biomimetic adhesive materials and anti-fouling strategies. STATEMENT OF SIGNIFICANCE: Discovering macromolecules and studying their associated mechanisms involved in underwater adhesion are essential for understanding the fundamental ecology of benthos in aquatic ecosystems and developing innovative bionic adhesive materials in various industries. Using multidisciplinary analytical methods, we identified an interfacial protein -
Ascidian Adhesive Protein 1 (AAP1) from the model marine fouling
ascidian, Ciona robusta. The interfacial functions of AAP1 are achieved by electrostatic and hydrophobic interactions, and the Von Willebrand factor type A domain-based cross-linking likely enhances AAP1\'s interfacial adhesion. The identification and validation of the interfacial functions of AAP1, combined with the elucidation of adhesion mechanisms, present a promising target for the development of biomimetic adhesive materials and the formulation of effective anti-fouling strategies.