Designing Multifunctional Biomaterials via Protein Self‐Assembly

Solomonov, Aleksei; Kozell, Anna; Shimanovich, Ulyana

doi:10.1002/anie.202318365

Cited by 11 publications

(1 citation statement)

References 107 publications

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“…The epithelial cells in the middle-middle and anterior-middle sections secrete the sericin proteins 40,47 , which later serves as the fibers' coating layer, gluing them into a cocoon. Of note, liquid silk feedstock is highly unstable and outside the silk gland can aggregate spontaneously within seconds 48 , which represents a major limitation in the investigation of silk fiber formation mechanisms and in artificial silk fibers generation 20,49,50 . Thus, how silk proteins are stabilized inside the gland is an open scientific question that remains poorly understood.…”

Section: Introductionmentioning

confidence: 99%

The Natural Material Evolution and Stage-wise Assembly of Silk Along the Silk Gland

Brookstein,

Shimoni,

Eliaz

et al. 2024

Preprint

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Silk fibers, with their highly ordered structure and mechanically superb properties, are produced in arthropod glands at minimal energy input and ambient conditions, a remarkable feat yet to be achieved synthetically. Due to the high instability and shear sensitivity of the silk protein feedstock, understanding silk fiber formation has been largely limited toin-vitrostudies of certain gland sections, offering only a fragmented view of this process. Here, we monitor the whole silk feedstock processingin-situ, at the nano- to micron-scales, through imaging its progressive macromolecular assemblies and phase transitions along the entireBombyx morisilkworm silk gland. This is done by combining state-of-the-art microscopy techniques, such as cryogenic sample preparation, fixation, and imaging. Our work reveals that fibroin assembles into micron-sized spherical storage “compartments” in the posterior and middle gland sections, a state that ensures its stability and avoids premature fibrillation. These compartments undergo several structural transformations along the gland and eventually disassemble at the entry to the anterior section, before the silk feedstock spinning begins. The spinning itself commences via a series of structural transitions, from the alignment of protein chains in liquid feedstock, through the formation of several fibrillated nano-structures and, in the final stage, a network of cross-linked nano-bundles, which determines the structure and properties of the final microfiber. Importantly, the length of the anterior section of the silk gland enables such gradual and balanced structural transitions. This direct imaging of silk’s natural formation process can help formulate a template for the transformation of fibrillar proteins into synthetic bio-fibers.DedicationThis work is dedicated to the memory of Dr. Eyal Shimoni, who was a valued colleague and a dear friend. Eyal was a vital part of this research and was essential in shaping its direction. He will be deeply missed for his intellect, mindfulness, creativity, and unwavering dedication to scientific development. Though he is no longer with us, his influence and spirit continue to inspire us in our scientific pursuits. May his passion for discovery and commitment to excellence live on through this work.

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Section: Introductionmentioning

confidence: 99%

The Natural Material Evolution and Stage-wise Assembly of Silk Along the Silk Gland

Brookstein,

Shimoni,

Eliaz

et al. 2024

Preprint

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Metals at the Helm: Revolutionizing Protein Assembly and Applications

Duan,

Lv,

Zang

et al. 2024

Macromolecular Bioscience

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Protein assembly is an essential process in biological systems, where proteins self‐assemble into complex structures with diverse functions. Inspired by the exquisite control over protein assembly in nature, scientists have been exploring ways to design and assemble protein structures with precise control over their topologies and functions. One promising approach for achieving this goal is through metal coordination, which utilizes metal‐binding motifs to mediate protein‐protein interactions and assemble protein complexes with controlled stoichiometry and geometry. Metal coordination provides a modular and tunable approach for protein assembly and de novo structure design, where the metal ion acts as a molecular glue that holds the protein subunits together in a specific orientation. Metal‐coordinated protein assemblies have shown great potential for developing functional metalloproteinase, novel biomaterials and integrated drug delivery systems. In this review, an overview of the recent advances in protein assemblies benefited from metal coordination is provided, focusing on various protein arrangements in different dimensions including protein oligomers, protein nanocage and higher‐order protein architectures. Moreover, the key metal‐binding motifs and strategies used to assemble protein structures with precise control over their properties are highlighted. The potential applications of metal‐mediated protein assemblies in biotechnology and biomedicine are also discussed.

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Development of artificial photosystems based on designed proteins for mechanistic insights into photosynthesis

Serrano,

Echavarría,

Mejias

2024

Protein Science

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This review aims to provide an overview of the progress in protein‐based artificial photosystem design and their potential to uncover the underlying principles governing light‐harvesting in photosynthesis. While significant advances have been made in this area, a gap persists in reviewing these advances. This review provides a perspective of the field, pinpointing knowledge gaps and unresolved challenges that warrant further inquiry. In particular, it delves into the key considerations when designing photosystems based on the chromophore and protein scaffold characteristics, presents the established strategies for artificial photosystems engineering with their advantages and disadvantages, and underscores the recent breakthroughs in understanding the molecular mechanisms governing light‐harvesting, charge separation, and the role of the protein motions in the chromophore's excited state relaxation. By disseminating this knowledge, this article provides a foundational resource for defining the field of bio‐hybrid photosystems and aims to inspire the continued exploration of artificial photosystems using protein design.

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Designing Multifunctional Biomaterials via Protein Self‐Assembly

Cited by 11 publications

References 107 publications

The Natural Material Evolution and Stage-wise Assembly of Silk Along the Silk Gland

The Natural Material Evolution and Stage-wise Assembly of Silk Along the Silk Gland

Metals at the Helm: Revolutionizing Protein Assembly and Applications

Development of artificial photosystems based on designed proteins for mechanistic insights into photosynthesis

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