Protein Design for the Synthesis and Stabilization of Highly Fluorescent Quantum Dots

Aires, Antonio; Möller, Marco; Cortajarena, Aitziber L.

doi:10.1021/acs.chemmater.0c01484

Cited by 16 publications

(15 citation statements)

References 101 publications

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“…72 A final example on how protein systems can serve quantum dot biotemplating is offered by Aires and co-workers (Figure 4). 73 In this work, CdS quantum dots were constructed using protein scaffold based on CTPR. The resulting protein-CdS quantum dots (Prot-CdSQDs), prepared by a biological route at 37 °C, showed highly photoluminescent and photostable, with a longshelf life, high stability, and biocompatibility under physiological environments.…”

Section: Protein−metal Hybrids (Pmhs)mentioning

confidence: 99%

Metal–Protein Hybrid Materials with Desired Functions and Potential Applications

Saif

Yang

2021

ACS Appl. Bio Mater.

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Metal nanohybrids are fast emerging functional nanomaterials with advanced structures, intriguing physicochemical properties, and a broad range of important applications in current nanoscience research. Significant efforts have been devoted toward design and develop versatile metal nanohybrid systems. Among numerous biological components, diverse proteins offer avenues for making advanced multifunctional systems with unusual properties, desired functions, and potential applications. This review discusses the rational design, properties, and applications of metal–protein nanohybrid materials fabricated from proteins and inorganic components. The construction of functional biomimetic nanohybrid materials is first briefly introduced. The properties and functions of these hybrid materials are then discussed. After that, an overview of promising application of biomimetic metal–protein nanohybrid materials is provided. Finally, the key challenges and outlooks related to this fascinating research area are also outlined.

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Section: Protein−metal Hybrids (Pmhs)mentioning

confidence: 99%

Metal–Protein Hybrid Materials with Desired Functions and Potential Applications

Saif

Yang

2021

ACS Appl. Bio Mater.

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“… 54 , 55 To address this challenge, we recently investigated the design of a metal-coordination site based on four histidines into a CTPR repeat module and generated CTPR scaffolds with different numbers of units for the sustainable synthesis and stabilization of CdS QDs with improved fluorescent properties, photostability, and biocompatibility. 56 These protein–metal QDs hybrids were able to enter into living cells, showing great cell labeling capacity at very low doses, making them useful tools for biomedical applications.…”

Section: Engineering Protein–nanomaterials Hybrids Based On Ctpr Scaffoldsmentioning

confidence: 99%

Engineered Repeat Protein Hybrids: The New Horizon for Biologic Medicines and Diagnostic Tools

et al. 2021

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Conspectus The last decades have witnessed unprecedented scientific breakthroughs in all the fields of knowledge, from basic sciences to translational research, resulting in the drastic improvement of the lifespan and overall quality of life. However, despite these great advances, the treatment and diagnosis of some diseases remain a challenge. Inspired by nature, scientists have been exploring biomolecules and their derivatives as novel therapeutic/diagnostic agents. Among biomolecules, proteins raise much interest due to their high versatility, biocompatibility, and biodegradability. Protein binders (binders) are proteins that bind other proteins, in certain cases, inhibiting or modulating their action. Given their therapeutic potential, binders are emerging as the next generation of biopharmaceuticals. The most well-known example of binders are antibodies, and inspired by them researchers have developed alternative binders using protein design approaches. Protein design can be based on naturally occurring proteins in which, by means of rational design or combinatorial approaches, new binding interfaces can be engineered to obtain specific functions or based on de novo proteins emerging from state-of-the-art computational methodologies. Among the novel designed proteins, a class of engineered repeat proteins, the consensus tetratricopeptide repeat (CTPR) proteins, stand out due to their stability and robustness. The CTPR unit is a helix-turn-helix motif constituted of 34 amino acids, of which only 8 are essential to ensure correct folding of the structure. The small number of conserved residues of CTPR proteins leaves plenty of freedom for functional mutations, making them a base scaffold that can be easily and reproducibly tailored to endow desired functions to the protein. For example, the introduction of metal-binding residues (e.g., histidines, cysteines) drives the coordination of metal ions and the subsequent formation of nanomaterials. Additionally, the CTPR unit can be conjugated with other peptides/proteins or repeated in tandem to encode larger CTPR proteins with superhelical structures. These properties allow for the design of both binder and nanomaterial-coordination modules as well as their combination within the same molecule, making the CTPR proteins, as we have demonstrated in several recent examples, the ideal platform to develop protein–nanomaterial hybrids. Generally, the fusion of two distinct materials exploits the best properties of each; however, in protein–nanomaterial hybrids, the fusion takes on a new dimension as new properties arise. These hybrids have ushered the use of protein-based nanomaterials as biopharmaceuticals beyond their original therapeutic scope and paved the way for their use as theranostic agents. Despite several reports of protein-stabilized nanomaterials found in the literature, these systems offer limited control in the synthesis and properties of the grown nanomaterials, as the protein acts just as a stabilizing agent with no significant functional contribution. T...

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“…In previous works carried out in our group, engineered CTPR proteins with metal coordinating residues have been thoroughly employed for the in situ templating of photoluminescent NCs [17,18] and quantum dots (QDs). [19] Recently, the interest in tuning the photoluminescent properties of protein-coordinated metal NCs has yielded several works that assess the use of different amino acids and commonly used proteins as coordination agents. [20,21] However, these works are focused on natural proteins, in which it is not possible to control the protein sequence and structure in a systematic manner.…”

Section: Introductionmentioning

confidence: 99%

Tuning the Optical Properties of Au Nanoclusters by Designed Proteins

López‐Martínez

Gianolio

Garcia‐Orrit

et al. 2021

Advanced Optical Materials

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but also by the ligands coordinated to them, as reported in recent studies. [2] In this sense, the coordination of metal-NCs with biomolecules is an emerging area of research since this biomolecular capping can endow multiple capabilities to the NCs, including biocompatibility, stability in biological media, and biological functionality (e.g., binding and inhibitory functions) resulting in hybrid bionanomaterials with a plethora of potential applications. [3] In this context, it has been shown that the capping and stabilization of metal NCs with peptides and proteins affect the optical properties of the NCs and the interaction with living matter by means of specific biological interplay. [4] Taking into account the role of the stabilizing agents on the NCs properties, an extra level of tailoring can be achieved by exploiting protein engineering. Metal coordinating engineered proteins are strongly inspired by natural metalloproteins, whose metalbinding capabilities allow to perform multiple functions, such as storage and transport, [5,6] sensing, [7,8] or catalysis. [9,10] In this framework, designed repeat proteins emerged as an interesting option to display custom metal coordination sites. Repeat proteins can be used as building blocks due to their modularity, regular geometry, and small size; allowing the design of both simple, but also more complex supramolecular assemblies and multifunctional systems. [11][12][13][14] The possibility of adding tailored chemical Gold nanoclusters (AuNCs) are nanomaterials with interesting photoluminescent properties that can be endowed with biomolecular recognition and biocompatibility when stabilized with proteins. The interplay between the optical features of AuNCs and the function added by the protein makes them perfect candidates for generating hybrid protein-inorganic nanomaterials. Focusing on protein stabilized-AuNCs, hitherto most of the work has covered the use of natural proteins for in situ growth of AuNCs. However, the exploitation of design proteins for such endeavors enables fine-tuning of the photoluminescent assets of AuNCs. In this work, rational protein engineering of modular protein scaffolds is applied for capping of non-emissive, non-passivated naked AuNCs, resulting in a fast and easy method for the synthesis of customizable and emissive protein-AuNC nanomaterials. Tuning of the photoluminescent properties of the final hybrid module is obtained by appropriate choice of the coordination residues grafted on the same protein scaffold. The effects of ligands and coordination bonds are studied using time-resolved photo luminescence and X-ray absorbance spectroscopies, shedding light on the mechanisms behind the emerging properties of these hybrid materials. Moreover, the described versatile strategy opens new avenues for the synthesis of on-demand photoluminescent hybrids for a wide spectrum of optical applications.

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Protein Design for the Synthesis and Stabilization of Highly Fluorescent Quantum Dots

Cited by 16 publications

References 101 publications

Metal–Protein Hybrid Materials with Desired Functions and Potential Applications

Metal–Protein Hybrid Materials with Desired Functions and Potential Applications

Engineered Repeat Protein Hybrids: The New Horizon for Biologic Medicines and Diagnostic Tools

Tuning the Optical Properties of Au Nanoclusters by Designed Proteins

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