Peptide self-assembly: thermodynamics and kinetics

Abstract

Self-assembling systems play a significant role in physiological functions and have therefore attracted tremendous attention due to their great potential for applications in energy, biomedicine and nanotechnology. Peptides, consisting of amino acids, are among the most popular building blocks and programmable molecular motifs. Nanostructures and materials assembled using peptides exhibit important potential for green-life new technology and biomedical applications mostly because of their bio-friendliness and reversibility. The formation of these ordered nanostructures pertains to the synergistic effect of various intermolecular non-covalent interactions, including hydrogen-bonding, π-π stacking, electrostatic, hydrophobic, and van der Waals interactions. Therefore, the self-assembly process is mainly driven by thermodynamics; however, kinetics is also a critical factor in structural modulation and function integration. In this review, we focus on the influence of thermodynamic and kinetic factors on structural assembly and regulation based on different types of peptide building blocks, including aromatic dipeptides, amphiphilic peptides, polypeptides, and amyloid-relevant peptides.

Supramolecular Peptide/Polymer Hybrid Hydrogels for Biomedical Applications

“…Noncovalent interactions are relatively weak (2–250 kJ⋅mol −1 ), compared to covalent bonds (100–400 kJ⋅mol −1 ), but when combined synergistically they allow the assembly of stable and well‐defined structures . Although self‐assembly is mainly driven by these thermodynamic interactions, the influence of kinetic factors (ionic strength, concentration, solvent, temperature, and pH) can be used to regulate the final structure and integrate functionality, as they also influence the intermolecular interactions or change the energy barriers . The review by Yan and coworkers discusses examples of thermodynamic and kinetically controlled self‐assembling peptide systems where supramolecular hydrogels are considered kinetically trapped structures …”

Biocatalytic Self-Assembly of Tripeptide Gels and Emulsions

“…27 !The balance between kinetic and thermodynamic aspects of peptide assembly and gelation are still far from fully understood and are difficult to precisely control, despite continued investigation. [28][29] We recently demonstrated the possibility of stabilizing emulsions on-demand, by making use of a biocatalytically-triggered self-assembly of nanofibrous networks of aromatic peptide amphiphiles (Fmoc-peptides) at the aqueous/organic interface. 30 However, Fmoc-peptide amphiphiles contain a non-biological component, which may not be acceptable for specific applications (cosmetics, food, etc.).…”

From self‐assembled peptide‐ynes to peptide polyacetylenes and polydiacetylenes

“…Whether peptides are made up exclusively of amino acids or are hybridized with other functional moieties (i.e., polymerizable sites), they are known to adopt well specific conformations and interesting self‐assembly morphologies, thus providing useful platforms for the development of nanoscale materials . Over the last decade, this class of hybrid compounds was extensively investigated by combining their routinely easy peptide synthesis and the possibility to conveniently design a specific secondary structure which may possess a precise function …”