Peptide Self-Assembled Nanostructures: From Models to Therapeutic Peptides

Gatto, Emanuela; Toniolo, Claudio; Venanzi, Mariano

doi:10.3390/nano12030466

Cited by 27 publications

(20 citation statements)

References 107 publications

(132 reference statements)

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“…Decoherence in peptides and proteins as a function of time can be assessed by known techniques, such as those used in studying light harvesting molecules [ 23 , 24 , 25 ]. It is not, at present, clear how to directly study the intensity of Quantum Zeno effects within a peptide, however it is reasonable to propose that if the atoms in a peptide form a collectively actualizing set, that QZE interactions will increase monotonically with the number of atoms in the system.…”

Section: Discussionmentioning

confidence: 99%

A Testable Theory for the Emergence of the Classical World

Kauffman

Patra

2022

Entropy

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The transition from the quantum to the classical world is not yet understood. Here, we take a new approach. Central to this is the understanding that measurement and actualization cannot occur except on some specific basis. However, we have no established theory for the emergence of a specific basis. Our framework entails the following: (i) Sets of N entangled quantum variables can mutually actualize one another. (ii) Such actualization must occur in only one of the 2N possible bases. (iii) Mutual actualization progressively breaks symmetry among the 2N bases. (iv) An emerging “amplitude” for any basis can be amplified by further measurements in that basis, and it can decay between measurements. (v) The emergence of any basis is driven by mutual measurements among the N variables and decoherence with the environment. Quantum Zeno interactions among the N variables mediates the mutual measurements. (vi) As the number of variables, N, increases, the number of Quantum Zeno mediated measurements among the N variables increases. We note that decoherence alone does not yield a specific basis. (vii) Quantum ordered, quantum critical, and quantum chaotic peptides that decohere at nanosecond versus femtosecond time scales can be used as test objects. (viii) By varying the number of amino acids, N, and the use of quantum ordered, critical, or chaotic peptides, the ratio of decoherence to Quantum Zeno effects can be tuned. This enables new means to probe the emergence of one among a set of initially entangled bases via weak measurements after preparing the system in a mixed basis condition. (ix) Use of the three stable isotopes of carbon, oxygen, and nitrogen and the five stable isotopes of sulfur allows any ten atoms in the test protein to be discriminably labeled and the basis of emergence for those labeled atoms can be detected by weak measurements. We present an initial mathematical framework for this theory, and we propose experiments.

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Section: Discussionmentioning

confidence: 99%

A Testable Theory for the Emergence of the Classical World

Kauffman

Patra

2022

Entropy

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“…A well-designed amino acid sequence can propagate, producing a variety of secondary structures (i.e., helices, sheets, and turns), which can form 3D architectures (i.e., fibrils, tapes, and nanotubes). 3 This approach enables control of the pathway that leads from the peptide building block to peptide-based smart materials showing specific functions. 4 The main challenge in the construction of novel functional peptide-based biomaterials is to design constituent peptide monomers that employ these unique secondary structural conformations to establish complementary surfaces that interact noncovalently in a reproducible manner to create the desired nanostructures with favorable properties.…”

Section: Introductionmentioning

confidence: 99%

The application of the hierarchical approach for the construction of foldameric peptide self-assembled nanostructures

Szefczyk,

Szulc,

Gąsior-Głogowska

et al. 2023

Soft Matter

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“…10−13 Nanocomponents formed by the self-assembly of bound peptides have been widely used in various fields. 4,14,15 MBPs provide a simple and versatile approach to bioembedding for material functionalization that is simpler and more effective than existing bioconjugation techniques, such as the EDC (1-ethyl-3- [3-(dimethylamino)propyl] carbodiimide hydrochloride) and NHS (N-hydroxysuccinimide). 16 Moreover, peptide-based materials show more powerful application potential in the synthesis of nanomaterials, such as guiding the self-assembly of nanomaterials, improving the biocompatibility of inorganic nanomaterials, and enabling in vivo applications.…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, traditional bioconjugation technology is inefficient and does not meet the requirements of clinical and technological applications. − Peptides are potential nanomaterial synthesis tools, which hold great promise for the development of nanotechnology. − MBPs are green and advanced targeted adhesives that can be used to functionalize the surface of various solid materials (Figure ). − Nanocomponents formed by the self-assembly of bound peptides have been widely used in various fields. ,, MBPs provide a simple and versatile approach to bioembedding for material functionalization that is simpler and more effective than existing bioconjugation techniques, such as the EDC (1-ethyl-3-[3-(dimethylamino)propyl] carbodiimide hydrochloride) and NHS ( N -hydroxysuccinimide) . Moreover, peptide-based materials show more powerful application potential in the synthesis of nanomaterials, such as guiding the self-assembly of nanomaterials, improving the biocompatibility of inorganic nanomaterials, and enabling in vivo applications .…”

Section: Introductionmentioning

confidence: 99%

Applications of Material-Binding Peptides: A Review

Ruan

Sohail

Zhao

et al. 2022

ACS Biomater. Sci. Eng.

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Material-binding peptides (MBPs) are functionalized adhesive materials consisting of a few to several dozen amino acids. This affinity between MBPs and materials is regulated by multiple interactions, including hydrogen bonding, electrostatic, hydrophobic interactions, and π–π stacking. They show selective binding and high affinity to a diverse range of inorganic and organic materials, such as silicon-based materials, metals, metal compounds, carbon materials, and polymers. They are used to improve the biocompatibility of materials, increase the efficiency of material synthesis, and guide the controlled synthesis of nanomaterials. In addition, these can be used for precise targeting of proteins by conjugating to target biomolecules. In this review, we summarize the main designs and applications of MBPs in recent years. The discussions focus on more efficient and functional peptides, including evolution and overall design of MBPs. We have also highlighted the recent applications of MBPs, such as functionalization of material surfaces, synthesis of nanomaterials, drug delivery, cancer therapy, and plastic degradation. Besides, we also discussed the development trend of MBPs. This interpretation will accelerate future investigations to bottleneck the drawbacks of available MBPs, promoting their commercial applications.

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Peptide Self-Assembled Nanostructures: From Models to Therapeutic Peptides

Cited by 27 publications

References 107 publications

A Testable Theory for the Emergence of the Classical World

A Testable Theory for the Emergence of the Classical World

The application of the hierarchical approach for the construction of foldameric peptide self-assembled nanostructures

Applications of Material-Binding Peptides: A Review

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