POS4-0260
Molecular-Level Investigation of Multi-Component Peptide Assembly
Topic
S4. Colloids, Interfaces, and Molecular Assemblies for Functional Soft Materials
When and Where
Sep 29, 2026
08:30 - 09:30
Room 301 (Grand Ballroom)
Session Chairs
Hae Jung SON
Boseok KANG
Presenter(s)
Nayeong Jeon (Max Planck Institute for Polymer Research)
Co-Author(s)
Abstract
Natural supramolecular systems are rarely composed of a single component. Instead, biological structures and functions emerge from interactions among multiple molecular species with distinct identities and assembly preferences. Understanding how these components recognize one another and organize into higher-order structures is important for deciphering biological systems and designing multi-component materials.
Multi-component peptide systems provide a versatile platform for addressing these questions. Depending on molecular compatibility and assembly conditions, peptide components may co-assemble, self-sort, or interfere with each other’s assembly. However, the mechanisms selecting these pathways remain difficult to resolve because such systems are dynamic and heterogeneous.
In this work, nuclear magnetic resonance (NMR) spectroscopy is employed to investigate molecular interactions underlying assembly in multi-component peptide systems. Because peptide assembly is strongly influenced by the functional groups present and their arrangement along the sequence, residue-specific analysis is essential for understanding how sequence controls recognition, solvation, and packing. NMR enables interaction-sensitive residues to be identified and linked to assembly behavior.
The results show that sequence arrangement influences assembly from the earliest stages of molecular recognition. Distinct residue-specific interactions emerge even before assembly and are reflected in peptide mobility, structural organization, and thermodynamic behavior observed from the complementary characterization. Even peptides with similar composition can follow different pathways because residue arrangement changes the balance of interactions.
This work aims to provide a mechanistic framework for understanding how molecular interactions govern assembly pathways and structures in complex peptide mixtures, thereby contributing to the rational design of multi-component peptide materials.
Multi-component peptide systems provide a versatile platform for addressing these questions. Depending on molecular compatibility and assembly conditions, peptide components may co-assemble, self-sort, or interfere with each other’s assembly. However, the mechanisms selecting these pathways remain difficult to resolve because such systems are dynamic and heterogeneous.
In this work, nuclear magnetic resonance (NMR) spectroscopy is employed to investigate molecular interactions underlying assembly in multi-component peptide systems. Because peptide assembly is strongly influenced by the functional groups present and their arrangement along the sequence, residue-specific analysis is essential for understanding how sequence controls recognition, solvation, and packing. NMR enables interaction-sensitive residues to be identified and linked to assembly behavior.
The results show that sequence arrangement influences assembly from the earliest stages of molecular recognition. Distinct residue-specific interactions emerge even before assembly and are reflected in peptide mobility, structural organization, and thermodynamic behavior observed from the complementary characterization. Even peptides with similar composition can follow different pathways because residue arrangement changes the balance of interactions.
This work aims to provide a mechanistic framework for understanding how molecular interactions govern assembly pathways and structures in complex peptide mixtures, thereby contributing to the rational design of multi-component peptide materials.
