12 – Self-assembly of peptides and its potential application

TLDR: In this paper, molecular self-assembly is defined as the spontaneous organization of molecules under near thermodynamic equilibrium conditions into structurally well-defined and stable arrangements through non-covalent interactions such as hydrogen bonding, electrostatic attraction, and van der Walls interactions.

Abstract: Publisher Summary Molecular self-assembly is the spontaneous organization of molecules under near thermodynamic equilibrium conditions into structurally well-defined and stable arrangements through non-covalent interactions. Such interactions typically include hydrogen bonding, electrostatic attraction, and van der Walls interactions. Frequently, molecular self assembly relies on chemical complementarity and structural compatibility. These fundamentals are critical to the design of molecular building blocks required for the fabrication of functional macrostructures. Molecular fabrication involves not only the understanding of molecular self-assembly, but also the knowledge of surface science. Materials communicate with their environment via their interfaces. Such communications are determined by the interfacial properties of the materials. In particular, understanding the molecular mechanisms and signaling cascades between living cells and their environment is crucial to fabricate novel biomaterials; biomineralization requires functional templates to direct and regulate the mineral deposition and the crystal growth. The molecular interactions in molecular self-assembly, in guest-host molecular recognition, and in molecular biomimetics are governed by the interfacial communications, which eventually control the material structures and their mechanical, electronic, magnetic, and solution properties.