The non-covalent decoration of self-assembling protein fibers

Mahmoud, Zahra N.; Grundy, Daniel J.; Channon, Kevin J.; Woolfson, Derek N.

doi:10.1016/j.biomaterials.2010.06.041

Cited by 37 publications

(38 citation statements)

References 29 publications

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“…24,31,32,[37][38][39][40][41][42][43] The nano-range dimensions constitute a key advantage, since their scale roughly matches the size of biological molecules, allowing promising developments. 10,44,45 It encompasses the study and monitoring of individual biomolecules under biologically relevant conditions. [45][46][47] It is now possible to track a biomolecule, such as a protein, in its biological context, for example when it interacts with a ligand inside a cell.…”

Section: Introductionmentioning

confidence: 99%

Amyloid-based nanosensors and nanodevices

2014

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Self-assembling amyloid-like peptides and proteins give rise to promising biomaterials with potential applications in many fields. Amyloid structures are formed by the process of molecular recognition and self-assembly, wherein a peptide or protein monomer spontaneously self-associates into dimers and oligomers and subsequently into supramolecular aggregates, finally resulting in condensed fibrils. Mature amyloid fibrils possess a quasi-crystalline structure featuring a characteristic fiber diffraction pattern and have well-defined properties, in contrast to many amorphous protein aggregates that arise when proteins misfold. Core sequences of four to seven amino acids have been identified within natural amyloid proteins. They are capable to form amyloid fibers and fibrils and have been used as amyloid model structures, simplifying the investigations on amyloid structures due to their small size. Recent studies have highlighted the use of self-assembled amyloid-based fibers as nanomaterials. Here, we discuss the latest advances and the major challenges in developing amyloids for future applications in nanotechnology and nanomedicine, with the focus on development of sensors to study protein-ligand interactions.

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Section: Introductionmentioning

confidence: 99%

Amyloid-based nanosensors and nanodevices

2014

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“…4). The film is generated through coassembly for functionalization of βFP [38,46–49]. We have shown that the EAK16-II/EAKIIH6 composite prolongs in vivo retention of IgG in inflammatory tissues, in mammary tumors implanted in syngeneic mice [29], and in tissues underneath skin allografts [30].…”

Section: Discussionmentioning

confidence: 99%

Local retention of antibodies in vivo with an injectable film embedded with a fluorogen-activating protein

Liu

Saunders

Bagia

et al. 2016

Journal of Controlled Release

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Herein we report an injectable film by which antibodies can be localized in vivo. The system builds upon a bifunctional polypeptide consisting of a fluorogen-activating protein (FAP) and a β-fibrillizing peptide (βFP). The FAP domain generates fluorescence that reflects IgG binding sites conferred by Protein A/G (pAG) conjugated with the fluorogen malachite green (MG). A film is generated by mixing these proteins with molar excess of EAK16-II, a βFP that forms β-sheet fibrils at high salt concentrations. The IgG-binding, fluorogenic film can be injected in vivo through conventional needled syringes. Confocal microscopic images and dose–response titration experiments showed that loading of IgG into the film was mediated by pAGMG bound to the FAP. Release of IgG in vitro was significantly delayed by the bioaffinity mechanism; 26% of the IgG were released from films embedded with pAGMG after five days, comparedto close to 90% in films without pAGMG. Computational simulations indicated that the release rate of IgG is governed by positive cooperativity due to pAGMG. When injected into the subcutaneous space of mouse footpads, film-embedded IgG were retained locally, with distribution through the lymphatics impeded. The ability to track IgG binding sites and distribution simultaneously will aid the optimization of local antibody delivery systems.

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“…Mahmoud et al demonstrated a non‐covalent labelling strategy using a negatively charged peptide ( DEDEDE ) as an anchor to bind to SAF , while neither neutral peptide ( AQAQAQ ) nor positively charged peptide ( KRKRKR ) exhibited strong binding ability. Non‐covalent modification with fluorophores or gold nanoparticles was visualized using light microscopy and TEM , respectively . To avoid the potential drawback of nonspecific binding with the anchor peptide, a biocompatible ‘click’ reaction was also employed by introducing azide functional groups directly within the SAF .…”

Section: Coiled‐coil Peptide Nanofiber Decoration For Biological Applmentioning

confidence: 99%

α‐Helical coiled‐coil peptide materials for biomedical applications

Collier

2016

WIREs Nanomed Nanobiotechnol

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Self-assembling coiled coils, which occur commonly in native proteins, have received significant interest for the design of new biomaterials-based medical therapies. Considerable effort over recent years has led to a detailed understanding of the self-assembly process of coiled coils, and a diverse collection of strategies have been developed for designing functional materials using this motif. The ability to engineer the interface between coiled coils allows one to achieve variously connected components, leading to precisely defined structures such as nanofibers, nanotubes, nanoparticles, networks, gels, and combinations of these. Currently these materials are being developed for a range of biotechnological and medical applications, including drug delivery systems for controlled release, targeted nanomaterials, “drug-free” therapeutics, vaccine delivery systems, and others.

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The non-covalent decoration of self-assembling protein fibers

Cited by 37 publications

References 29 publications

Amyloid-based nanosensors and nanodevices

Amyloid-based nanosensors and nanodevices

Local retention of antibodies in vivo with an injectable film embedded with a fluorogen-activating protein

α‐Helical coiled‐coil peptide materials for biomedical applications

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