(168k) Engineering Amyloid Inspired Peptides for Tunable Assembly

Amyloid proteins have provided inspiration for developing functional materials due to their stability against mechanical, thermal and chemical factors. These amyloid based assemblies allow scientist to mimic the nature of amyloid structures to build amyloid inspired hierarchical synthetic structures for different applications such as drug delivery, tissue engineering and energy-based materials.¹ The stability of Ab (1-42) was mainly derived from two different interactions which are salt bridges and hydrophobic clusters found in the core of protein. However, there is not still any general rule or method to understand the assembly kinetics and screen intermolecular interactions. In this research, we present a simplistic tool (Figure 1) consisting of oppositely charged hexapeptide to identify the effect of hydrophobicity and salt-bridges on aggregation kinetics and physical properties of final material such as secondary structures and mechanical properties.²Computational and experimental approaches show that salt bridges are required for peptide fibrillization and the distance of undistrupted hydrophobic core in co-assembly has a strong effect on assembly kinetics, overall stability, fibrillar morphology, mechanical properties and structural organization.

References

1. Wei, G. et al. Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology. Chemical Society Reviews 46, 4661–4708 (2017).
2. Hamsici, S., White, A. D. & Acar, H. Peptide framework for screening the effects of amino acids on assembly. Science Advances (2022) doi:10.1126/sciadv.abj0305.