Coiled coil-based therapeutics and drug delivery systems

Utterström, Johanna; Naeimipour, Sajjad; Selegård, Robert; Aili, Daniel

doi:10.1016/j.addr.2020.12.012

Cited by 44 publications

(47 citation statements)

References 151 publications

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“…ANKIB1 also contains a coiled-coil motif in its Ariadne domain. Similar to the ANK domain, coiled-coil is a ubiquitous protein motif that mediates protein-protein interactions among a wide range of proteins and has been widely used in medical research [25]. Both ankyrin-repeat and coiled-coil domain can self-associate [6].…”

Section: Discussionmentioning

confidence: 99%

ANKIB1 Functions as a Partner of E3 ubiquitin ligase 

Xie¹,

Ma²,

Yang³

et al. 2021

Preprint

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ANKIB1 is an RBR domain-containing protein. It has been classified as an E3 ubiquitin ligase for a long time. However, little is known about its E3 ligase activity and related ubiquitin-conjugating enzymes (E2s). We investigated the expression pattern, cellular localization, and brain distribution of ANKIB1. Immunoblotting showed that human cancer cell lines had different expression patterns of ANKIB1 with virus-transformed immortal lymphocytes and human brain. Immunocytofluorescence analysis indicated that ANKIB1 was mainly localized in the cytoplasm, and immunohistochemistry staining demonstrated that ANKIB1 was highly expressed in the rat brain cortex but seldom expressed in the basal ganglia. We then performed coimmunoprecipitation, in vitro and in vivo ubiquitination assay to determine whether ANKIB1 functions as an E3 ligase. A panel of class I and class III E2s were tested, of which UbcH8, UbcH10, and UbcH13 were confirmed to interact with ANKIB1. Moreover, ANKIB1 showed E3 ligase activity both in vivo and in vitro, but it promoted protein ubiquitination more efficiently in vivo. These data suggest that ANKIB1 acts as a partner of an E3 ligase complex, and may play important roles in regulating tumorigenesis and brain cortex function.

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Section: Discussionmentioning

confidence: 99%

ANKIB1 Functions as a Partner of E3 ubiquitin ligase 

Xie¹,

Ma²,

Yang³

et al. 2021

Preprint

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“…The feasibility of multitarget labeling with orthogonal coils was demonstrated with SYNZIP coils labeling of extracellular membrane proteins [107]. Multiple orthogonal coiled-coils were recently reported [111][112][113] and used, for example, in drug delivery systems [114], paving the way to future implementations of multitarget labeling.…”

Section: Imaging By Peptide-peptide Interactionsmentioning

confidence: 99%

Transient Fluorescence Labeling: Low Affinity—High Benefits

Perfilov

Gavrikov

Lukyanov

et al. 2021

IJMS

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Fluorescent labeling is an established method for visualizing cellular structures and dynamics. The fundamental diffraction limit in image resolution was recently bypassed with the development of super-resolution microscopy. Notably, both localization microscopy and stimulated emission depletion (STED) microscopy impose tight restrictions on the physico-chemical properties of labels. One of them—the requirement for high photostability—can be satisfied by transiently interacting labels: a constant supply of transient labels from a medium replenishes the loss in the signal caused by photobleaching. Moreover, exchangeable tags are less likely to hinder the intrinsic dynamics and cellular functions of labeled molecules. Low-affinity labels may be used both for fixed and living cells in a range of nanoscopy modalities. Nevertheless, the design of optimal labeling and imaging protocols with these novel tags remains tricky. In this review, we highlight the pros and cons of a wide variety of transiently interacting labels. We further discuss the state of the art and future perspectives of low-affinity labeling methods.

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“…First, the largest proportion of folded and active protein in these assemblies should permit reducing the critical concentrations for in vivo administration and the production costs. Additionally, lower doses would diminish undesired side effects, which, together with the lack of significant intrinsic toxicity demonstrated for coiled-coil based nanoparticles (Utterström et al, 2021), would make α-helix-rich IBs safer protein nanoparticles, mainly because they are expected to be devoid of potentially toxic β-sheet sustained conformations. Finally, because the native-like intermolecular interactions sustaining coiled-coil IBs are expected to be less robust than the strong amyloid-like contacts that glue β-sheet IBs (Carrió et al, 2005), these nanoparticles could display a higher release-efficiency upon their administration.…”

Section: Biomedical and Biotechnological Applications Of Functional Ibs: Is There Room For Improvement?mentioning

confidence: 99%

Coiled-Coil Based Inclusion Bodies and Their Potential Applications

Gil-García

Ventura

2021

Front. Bioeng. Biotechnol.

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The production of recombinant proteins using microbial cell factories is frequently associated with the formation of inclusion bodies (IBs). These proteinaceous entities can be sometimes a reservoir of stable and active protein, might display good biocompatibility, and are produced efficiently and cost-effectively. Thus, these submicrometric particles are increasingly exploited as functional biomaterials for biotechnological and biomedical purposes. The fusion of aggregation-prone sequences to the target protein is a successful strategy to sequester soluble recombinant polypeptides into IBs. Traditionally, the use of these IB-tags results in the formation of amyloid-like scaffolds where the protein of interest is trapped. This amyloid conformation might compromise the protein’s activity and be potentially cytotoxic. One promising alternative to overcome these limitations exploits the coiled-coil fold, composed of two or more α-helices and widely used by nature to create supramolecular assemblies. In this review, we summarize the state-of-the-art of functional IBs technology, focusing on the coiled-coil-assembly strategy, describing its advantages and applications, delving into future developments and necessary improvements in the field.

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Coiled coil-based therapeutics and drug delivery systems

Cited by 44 publications

References 151 publications

ANKIB1 Functions as a Partner of E3 ubiquitin ligase

ANKIB1 Functions as a Partner of E3 ubiquitin ligase

Transient Fluorescence Labeling: Low Affinity—High Benefits

Coiled-Coil Based Inclusion Bodies and Their Potential Applications

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Coiled coil-based therapeutics and drug delivery systems

Cited by 44 publications

References 151 publications

ANKIB1 Functions as a Partner of E3 ubiquitin ligase&nbsp;

ANKIB1 Functions as a Partner of E3 ubiquitin ligase&nbsp;

Transient Fluorescence Labeling: Low Affinity—High Benefits

Coiled-Coil Based Inclusion Bodies and Their Potential Applications

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Product

Resources

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ANKIB1 Functions as a Partner of E3 ubiquitin ligase

ANKIB1 Functions as a Partner of E3 ubiquitin ligase