The Dominant Role of Oxygen in Modulating the Chemical Evolution Pathways of Tyrosine in Peptides: Dityrosine or Melanin

Ren, Xiaokang; Zou, Qianli; Yuan, Chengqian; Chang, Rui; Xing, Ronge; Yan, Xuehai

doi:10.1002/anie.201814575

Cited by 77 publications

(44 citation statements)

References 50 publications

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“…[ 34 ] Peptide self‐assembly is affected by many factors that, in turn, serve as methods for regulating biological function of the peptide assemblies. [ 35 ] In addition, supramolecular peptide assemblies can incorporate a variety of functional components to form immunotherapeutic materials on demand. [ 36 ] These peptide assemblies increase molecular weight and stability in vivo due to the formation of aggregates, extend circulation time in vivo, increase cellular uptake, and are able to fuse responsive components to improve self‐adaptability in vivo and increase functionality.…”

Section: Supramolecular Peptide Immunotherapymentioning

confidence: 99%

Supramolecular Immunotherapy of Cancer Based on the Self‐Assembling Peptide Design

Chang

Yan

2020

Small Structures

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Supramolecular peptide assemblies with specific motifs have the advantages of high immunogenicity, regulated immune response, and increased multiple functions in improving the performance of cancer immunotherapy, compared with molecular peptide immunotherapy. These peptide-based assemblies with structural and functional versatility can serve as immunotherapeutic agents such as antigens, adjuvants, drug delivery carriers, or immunomodulators. This article reviews the effects of supramolecular peptide assemblies on cancer immunotherapy and highlights the unique role of supramolecular assembly strategies in regulating the immunotherapeutic performance. The mechanism of how the peptide supramolecular self-assembly affects the performance of immunotherapy is critically emphasized. The summary of peptide supramolecular immunotherapy provides a reference for the precise design of adjustable and multifunctional immunotherapeutic agents, and shows that peptide self-assembly has great application prospects in cancer immunotherapy.

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Section: Supramolecular Peptide Immunotherapymentioning

confidence: 99%

Supramolecular Immunotherapy of Cancer Based on the Self‐Assembling Peptide Design

Chang

Yan

2020

Small Structures

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“…This suggests that oxidized GYK forms are required for fluorescence. However, the greater oxidization of tyrosine under higher concentrations of H 2 O 2 may result in a different chemical pathway to an intermediate for formation of melanin‐like components, which could be less fluorescent and also act as quenchers for the coexisting fluorescent nanostructures …”

Section: Figurementioning

confidence: 99%

“…2.0 nm) exist in the third fraction (Figure G), as verified by both atomic force microscopy (AFM, Figure H) and transmission electron microscopy (TEM, Figure I). These large structures could be either covalently cross‐linked melanin‐like polymers or assembled nanostructures, with the blue‐shifted fluorescence induced by the aggregation effect …”

Section: Figurementioning

confidence: 99%

Generating Cyan Fluorescence with De Novo Tripeptides: An In Vitro Mutation Study on the Role of Single Amino Acid Residues and Their Sequence

et al. 2019

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Amino acids are natural choices as building blocks when developing biofunctional entities owing to their superior diversity and versatile physicochemical properties compared to nucleotide bases. A simple permutation of the amino acids creates a broad palette of proteins and these have been successfully engineered into useful biofunctional agents. For example, the intrinsic ultraviolet fluorescence of phenylalanine and tryptophan has been engineered to emit in the visible spectrum, which has broad applications for imaging/sensing probes, photothermal therapy agents, optogenetic switches, etc. Nature produces more colorful coats/furs, feathers/hairs, and eyes through various biochemical modifications of tyrosine‐based pigmentation. However, it is challenging to modulate the fluorescence wavelength from the UV to the visible region through oligopeptides. Herein, we report an innovative approach to obtain cyan fluorescence by using de novo tripeptides containing glycine, tyrosine, and lysine, which form robust dimer structures under moderate oxidizing conditions. Through an in vitro mutation approach, we deduce that both the amino acids and their sequence play significant roles in modulating the fluorescence. We believe this work holds great promise for developing novel cell imaging and resonance energy‐transfer‐based fluorescent probes.

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“…28 Other derivatives of tyrosine were also shown to exhibit luminescence upon aggregation. 29 Yet, the underlying mechanism of the autofluorescence of these assemblies is controversial, as in all cases it can be attributed to the aromatic moiety. In addition, the explanation of impurities as the source of fluorescence is still a plausible option.…”

Section: Introductionmentioning

confidence: 99%

On-off transition and ultrafast decay of amino acid luminescence driven by modulation of supramolecular packing

Arnon

Kreiser

Yakimov

et al. 2021

Preprint

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It has been experimentally observed that various biomolecules exhibit clear luminescence in the visible upon aggregation, contrary their monomeric state. However, the physical basis for this phenomenon is still elusive. Here, we systematically examine all coded amino acids to provide non-biased insights into this phenomenon. Several amino acids, including non-aromatic, show intense visible luminescence. While lysine crystals display the highest signal, the very chemically similar non-coded ornithine does not, implying a role for molecular packing rather than the chemical characteristics of the molecule. Furthermore, cysteine show luminescence that is indeed crystal-packing-dependent as repeated rearrangements between two crystal structures result in a reversible on-off optical transition. In addition, ultrafast lifetime decay is experimentally validated, corroborating a recently raised hypothesis regarding the governing role of nπ* states in the emission formation. Collectively, our study supports the hypothesis that electronic interactions between molecules that are non-fluorescent and non-absorbing at the monomeric state may result in reversible optically-active states by the formation of supramolecular fluorophores.

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The Dominant Role of Oxygen in Modulating the Chemical Evolution Pathways of Tyrosine in Peptides: Dityrosine or Melanin

Cited by 77 publications

References 50 publications

Supramolecular Immunotherapy of Cancer Based on the Self‐Assembling Peptide Design

Supramolecular Immunotherapy of Cancer Based on the Self‐Assembling Peptide Design

Generating Cyan Fluorescence with De Novo Tripeptides: An In Vitro Mutation Study on the Role of Single Amino Acid Residues and Their Sequence

On-off transition and ultrafast decay of amino acid luminescence driven by modulation of supramolecular packing

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