Structure of supramolecular peptide assemblies

Seashells, diatom cell walls, and even bone are made by living systems that grow minerals with remarkable precision. They dont start with a lump of rock. Instead, they first assemble tiny peptide building blocks, short pieces of proteins, that come together into soft templates. These templates then guide mineral salts, such as silica, to form specific shapes and sizes. The project Structure of Supramolecular Peptide Self-Assemblies aims to decipher and understand the atomistic structure of the templates, enabling the eventual design of better biologically inspired materials. Although scientists have long studied biominerals, the very first steps, the formation of the soft, solution-phase templates, were not yet possible due to a lack of methods to access these complex systems. We will combine high-resolution magnetic resonance (NMR) measurements (the analytical form of medical MRI) with computer simulations to reconstruct these templates at the level of individual atoms. In simple terms: we listen to the tiny magnetic voices of the peptides in solution, build 3D models from those clues, and then validate our models with X-ray scattering and electron microscopy. If the predicted template produces the same silica particle shape that we see under the microscope, we know weve decoded the proper structure. Being able to read the template rules opens the door to creating cleaner, more innovative materials on purpose. Think of particles for drug delivery that carry medicines exactly where theyre needed, or catalysts that speed up reactions with less waste. Because these templates are inspired by biology and made under mild, water-based conditions, the resulting materials can be biocompatible and more sustainable. First, we utilize specialized NMR methods that can identify the signals of small peptide clusters even when theyre hidden within much larger assemblies. Second, we model our targets. We feed those signals into molecular dynamics simulations, letting the computer grow realistic templates from a handful of peptide units. Finally, we double-check the predicted shapes with small-angle X-ray scattering and electron microscopy; two powerful ways of seeing soft structures without destroying them. By the end, we aim to deliver a toolbox for decoding and designing peptide templates that reliably predict the final mineral shapes, from spheres to needles to plates, and to share clear rules that link peptide sequence to template and particle morphology. This knowledge will help researchers craft the next generation of eco-friendly, high-performance materials.