A Near‐Infrared Photoswitchable Protein–Fluorophore Tag for No‐Wash Live Cell Imaging

Sheng, Wei; Nick, Setare Tahmasebi; Santos, Elizabeth Moreira dos; Ding, Xinliang; Zhang, Jun; Vasileiou, Chrysoula; Geiger, James H.; Borhan, Babak

doi:10.1002/anie.201810065

Cited by 24 publications

(23 citation statements)

References 35 publications

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“…As targeting moieties, antibodies are limited due to their large size, complicated production methods and high cost. Small peptides offers an alternative strategy with lower immunogenicity and price of use as therapeutic agents or targeting groups for effective targeted cancer therapy . Targeting moieties, Arg‐Gly‐Asp (RGD) and Asn‐Gly‐Arg (NGR) have been used to interact with integrin avb3 (CD51/CD61) and aminopeptidyl N (CD13) receptors, which are highly expressed in angiogenic tumors or other tissues with angiogenic components .…”

Section: Peptide‐conjugated Nanomaterialsmentioning

confidence: 99%

Bio‐Conjugated Advanced Materials for Targeted Disease Theranostics

Kwon

Yan

et al. 2020

Adv Funct Materials

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Human beings are “machines” that use endogenously produced biomolecules as “components” in signaling and for the maintenance of the body. These biomolecules consist of proteins, nucleic acids, and carbohydrates, which can either be extracted from biological substrates or synthesized by chemical/biochemical methods. These biomolecules have the ability to recognize/interact with other biomolecules that are overexpressed in disease cells. For targeted theranostics, strategies to chemically incorporate these natural biomolecules with advanced materials to treat human diseases by imaging‐guided drug delivery or photodynamic/photothermal therapy are proposed, with improved biocompatibility. Herein, recent research on construction of quantum dots, nanoparticles, and 2D material platforms decorated with antibodies, peptides, nucleic acid aptamers, carbohydrates, and folic acid for targeted diagnosis and treatment are summarized and discussed. In addition, the various strategies required to construct effective functional materials for targeted cancer therapy are highlighted. The hope is that this review can inspire and guide those that are interested in the field of biomedicine to rationally design and develop new target‐based theranostic materials.

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Section: Peptide‐conjugated Nanomaterialsmentioning

confidence: 99%

Bio‐Conjugated Advanced Materials for Targeted Disease Theranostics

Kwon

Yan

et al. 2020

Adv Funct Materials

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“…Human cellular retinol binding protein II (hCRBPII) chaperones both retinol and retinal within the cell. Our group has engineered these templates to create rhodopsin mimics used to understand protein‐based absorption tuning, protein‐directed photoisomerization pathways, [35–37] new classes of fluorescent and photoswitchable fluorescent protein tags, [38] and pH sensors [39,40] . We recently reported that some variants of hCRBPII give rise to domain‐swapped (DS) dimers [41] .…”

Section: Figurementioning

confidence: 99%

“…Our group has engineered these templates to create rhodopsin mimics used to understand protein-based absorption tuning, protein-directed photoisomerization pathways, [35][36][37] new classes of fluorescent and photoswitchable fluorescent protein tags, [38] and pH sensors. [39,40] We recently reported that some variants of hCRBPII give rise to domain-swapped (DS) dimers. [41] We then exploited the hCRBPII DS dimer as a design template to engineer a new class of protein conformational switches, activated by ligand binding or environmental reduction potential, characteristics lacking in the monomeric fold of the protein.…”

mentioning

confidence: 99%

Human Cellular Retinol Binding Protein II Forms a Domain‐Swapped Trimer Representing a Novel Fold and a New Template for Protein Engineering

et al. 2020

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Domain‐swapping is a mechanism for evolving new protein structure from extant scaffolds, and has been an efficient protein‐engineering strategy for tailoring functional diversity. However, domain swapping can only be exploited if it can be controlled, especially in cases where various folds can coexist. Herein, we describe the structure of a domain‐swapped trimer of the iLBP family member hCRBPII, and suggest a mechanism for domain‐swapped trimerization. It is further shown that domain‐swapped trimerization can be favored by strategic installation of a disulfide bond, thus demonstrating a strategy for fold control. We further show the domain‐swapped trimer to be a useful protein design template by installing a high‐affinity metal binding site through the introduction of a single mutation, taking advantage of its threefold symmetry. Together, these studies show how nature can promote oligomerization, stabilize a specific oligomer, and generate new function with minimal changes to the protein sequence.

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“…21,22 The donating uorene fragment allows for a high absorption cross section and accommodates efficient through-bond energy transfer to the acceptor fragment, which results in bright chromophores that emit at long wavelengths. [23][24][25] The central p-conjugated backbone is typically anked by a combination of hydrophobic and hydrophilic sidechains. The design of the central core largely dictates the uorescence emission prole, 26,27 while the nature of these sidechains inuences the self-assembly behavior in aqueous solution.…”

Section: Introductionmentioning

confidence: 99%