Molecular self-assembly is the spontaneous association of molecules under equilibrium conditions into stable, structurally well-defined aggregates joined by noncovalent bonds. Molecular self-assembly is ubiquitous in biological systems and underlies the formation of a wide variety of complex biological structures. Understanding self-assembly and the associated noncovalent interactions that connect complementary interacting molecular surfaces in biological aggregates is a central concern in structural biochemistry. Self-assembly is also emerging as a new strategy in chemical synthesis, with the potential of generating nonbiological structures with dimensions of 1 to 10(2) nanometers (with molecular weights of 10(4) to 10(10) daltons). Structures in the upper part of this range of sizes are presently inaccessible through chemical synthesis, and the ability to prepare them would open a route to structures comparable in size (and perhaps complementary in function) to those that can be prepared by microlithography and other techniques of microfabrication.

Molecular self-assembly and nanochemistry: A chemical strategy for the synthesis of nanostructures

The self-assembling peptide EAK16-II is capable of stabilizing hydrophobic compounds to form microcrystal suspensions in aqueous solution. Here, the ability of this peptide to stabilize the hydrophobic anticancer agent ellipticine is investigated. The formation of peptide-ellipticine suspensions is monitored with time until equilibrium is reached. The equilibration time is found to be dependent on the peptide concentration. When the peptide concentration is close to its critical aggregation concentration, the equilibration time is minimal at 5 h. With different combinations of EAK16-II and ellipticine concentrations, two molecular states (protonated or cyrstalline) of ellipticine could be stabilized. These different states of ellipticine significantly affect the release kinetics of ellipticine from the peptide-ellipticine complex into the egg phosphatidylcholine vesicles, which are used to mimic cell membranes. The transfer rate of protonated ellipticine from the complex to the vesicles is much faster than that of crystalline ellipticine. This observation may also be related to the size of the resulting complexes as revealed from the scanning electron micrographs. In addition, the complexes with protonated ellipticine are found to have a better anticancer activity against two cancer cell lines, A549 and MCF-7. This work forms the basis for studies of the peptide-ellipticine suspensions in vitro and in vivo leading to future development of self-assembling peptide-based delivery of hydrophobic anticancer drugs.

Self‐Assembling Peptide as a Potential Carrier for Hydrophobic Anticancer Drug Ellipticine: Complexation, Release and In Vitro Delivery

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

Size-controlled Ni nanocrystal growth on peptide nanotubes and their magnetic properties

Beyond molecular chemistry based on the covalent bond, supramolecular chemistry aims at developing highly complex chemical systems from components interacting through noncovalent intermolecular forces. Over the past quarter century, supramolecular chemistry has grown into a major field and has fueled numerous developments at the interfaces with biology and physics. Some of the conceptual advances and future challenges are profiled here.

https://dialnet.unirioja.es/descarga/articulo/1051047.pdf

Toward self-organization and complex matter

Cancer is a devastating disease that causes a substantial number of deaths worldwide. Current therapeutic interventions for cancer include chemotherapy, radiation therapy, or surgery. These conventional therapeutic approaches are associated with disadvantages such as multidrug resistance, destruction of healthy tissues, and tissue toxicity. Therefore, there is a paradigm shift in cancer management wherein nanomedicine-based novel therapeutic interventions are being explored to overcome the aforementioned disadvantages. Supramolecular self-assembled peptide nanofibers are emerging drug delivery vehicles that have gained much attention in cancer management owing to their biocompatibility, biodegradability, biomimetic property, stimuli-responsiveness, transformability, and inherent therapeutic property. Supramolecules form well-organized structures via non-covalent linkages, the intricate molecular arrangement helps to improve tissue permeation, pharmacokinetic profile and chemical stability of therapeutic agents while enabling targeted delivery and allowing efficient tumor imaging. In this review, we present fundamental aspects of peptide-based self-assembled nanofiber fabrication their applications in monotherapy/combinatorial chemo- and/or immuno-therapy to overcome multi-drug resistance. The role of self-assembled structures in targeted/stimuli-responsive (pH, enzyme and photo-responsive) drug delivery has been discussed along with the case studies. Further, recent advancements in peptide nanofibers in cancer diagnosis, imaging, gene therapy, and immune therapy along with regulatory obstacles towards clinical translation have been deliberated. 

Supramolecular self-assembled peptide-engineered nanofibers: A propitious proposition for cancer therapy.

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.

12 – Self-assembly of peptides and its potential application

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12 – Self-assembly of peptides and its potential application