Unveiling the nanoscale architectures and dynamics of protein assembly with in situ atomic force microscopy DOI Creative Commons
Zhaoyi Zhai, Sakshi Yadav, Zhi-Xing Lin

et al.

Aggregate, Journal Year: 2024, Volume and Issue: 5(5)

Published: May 30, 2024

Abstract Proteins play a vital role in different biological processes by forming complexes through precise folding with exclusive inter‐ and intra‐molecular interactions. Understanding the structural regulatory mechanisms underlying protein complex formation provides insights into biophysical processes. Furthermore, principle of assembly gives guidelines for new biomimetic materials potential applications medicine, energy, nanotechnology. Atomic force microscopy (AFM) is powerful tool investigating interactions across spatial scales (single molecules to cells) temporal (milliseconds days). It has significantly contributed understanding nanoscale architectures, interactions, elements that determine structures, assemblies, functions. This review describes recent advancements elucidating assemblies situ AFM. We discuss diffusions, dynamics proteins captured conventional high‐speed AFM near‐native environments developments multimodal high‐resolution imaging, bimodal live cell machine‐learning‐enhanced data analysis. These approaches show significance broadening horizons enable unprecedented explorations biomaterial design biomedical research.

Language: Английский

Structural Ordering of Interfacially Assembled Silk Fibroin-Like Peptides via Robust Intermolecular Hydrogen-Bonding Networks DOI
Peiying Li, Chen Chen, Ayhan Yurtsever

et al.

ACS Materials Letters, Journal Year: 2024, Volume and Issue: 6(9), P. 3993 - 4001

Published: July 30, 2024

The formation of strong intermolecular hydrogen-bonding networks among repeating key motifs, i.e., Glu-Ala motifs silk fibroin proteins, providing excellent mechanical and biochemical properties, has gained broad attention in many fields. For example, biosensing, they could be utilized as stable molecular scaffolds on layered nanomaterials such MoS2 for high-sensitivity targeting-molecule detection. However, understanding the characteristics self-assembled fibroin-like concentration-/time-dependent morphological structural changes, solids is still poor. Moreover, length inducing hydrogen bonds, peptide sequences determining nucleation growth rates, controlling molecular-scale features not yet been explored. Thus, we synthetic peptides with NH2–Y(GA)n=3–5Y–COOH to investigate characteristics, orientations, single molecule structures under different time concentration conditions. This work would expand potential applications using peptide-based nanodevices biosensing bioelectronics.

Language: Английский

Citations

4
Deciphering Desorption Pathways and Mechanisms of Peptide Supramolecular Structures Thermodynamically and Kinetically by High-Speed AFM DOI Creative Commons
Linhao Sun, Jinhua Hu, Ayhan Yurtsever

et al.

ACS Central Science, Journal Year: 2025, Volume and Issue: unknown

Published: April 1, 2025

Language: Английский

Citations

0
Unveiling the nanoscale architectures and dynamics of protein assembly with in situ atomic force microscopy DOI Creative Commons
Zhaoyi Zhai, Sakshi Yadav, Zhi-Xing Lin

et al.

Aggregate, Journal Year: 2024, Volume and Issue: 5(5)

Published: May 30, 2024

Abstract Proteins play a vital role in different biological processes by forming complexes through precise folding with exclusive inter‐ and intra‐molecular interactions. Understanding the structural regulatory mechanisms underlying protein complex formation provides insights into biophysical processes. Furthermore, principle of assembly gives guidelines for new biomimetic materials potential applications medicine, energy, nanotechnology. Atomic force microscopy (AFM) is powerful tool investigating interactions across spatial scales (single molecules to cells) temporal (milliseconds days). It has significantly contributed understanding nanoscale architectures, interactions, elements that determine structures, assemblies, functions. This review describes recent advancements elucidating assemblies situ AFM. We discuss diffusions, dynamics proteins captured conventional high‐speed AFM near‐native environments developments multimodal high‐resolution imaging, bimodal live cell machine‐learning‐enhanced data analysis. These approaches show significance broadening horizons enable unprecedented explorations biomaterial design biomedical research.

Language: Английский

Citations

1