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Nanomaterials
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Protein Nanostructures for Biomedical Applications
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Protein Nanostructures for Biomedical Applications

A special issue of Nanomaterials (ISSN 2079-4991). This special issue belongs to the section "Biology and Medicines".

Deadline for manuscript submissions: closed (30 October 2020) | Viewed by 30703

Special Issue Editor

Dr. Christofer Lendel

E-Mail Website
Guest Editor
KTH Royal Institute of Technology, Department of Chemistry, Stockholm, Sweden
Interests: protein structure; protein self-assembly; amyloid; protein-based materials

Special Issue Information

Dear Colleagues,

It is a well-known fact that proteins are key players in essentially all biological processes and that protein molecules often are organized into functional nanoscale assemblies. Inspired by Nature’s design principles, protein-based nanostructures are becoming important components in a range of biomedical applications, including, for example, drug delivery, biosensors, and tissue engineering. The opportunity to tailor the structural and functional properties of protein molecules and their supramolecular assemblies offers design possibilities that are truly unique for proteins. The intrinsic biocompatibility of protein-based structures is indeed an attractive property for these technologies, but there are also important questions related to the potential risks of, for instance, amyloid-like protein nanofibrils, which need to be further investigated. This Special Issue of Nanomaterials invites contributions concerning the design, development or application of peptide- or protein-based nanostructures for biomedical purposes.

Dr. Christofer Lendel
Guest Editor

Manuscript Submission Information

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Keywords

  • protein nanostructures
  • functional nanomaterials
  • biomaterials
  • protein self-assembly
  • protein engineering and design
  • drug delivery
  • biosensors
  • tissue engineering

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Published Papers (7 papers)

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Research

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12 pages, 1985 KiB  
Article
Self-Assembled Multi-Epitope Peptide Amphiphiles Enhance the Immune Response against Enterovirus 71
by Yu-Gyeong Kim, Yunsu Lee, Joo Hee Kim, Sun-Young Chang, Jong-Wha Jung, Woo-Jae Chung and Hyo-Eon Jin
Nanomaterials 2020, 10(12), 2342; https://doi.org/10.3390/nano10122342 - 25 Nov 2020
Cited by 5 | Viewed by 2790
Abstract
Subunit vaccines consist of non-genetic material, such as peptides or proteins. They are considered safe because they have fewer side effects; however, they have low immunogenicity when used alone. We aimed to enhance the immune response of peptide-based vaccines by using self-assembled multimeric [...] Read more.
Subunit vaccines consist of non-genetic material, such as peptides or proteins. They are considered safe because they have fewer side effects; however, they have low immunogenicity when used alone. We aimed to enhance the immune response of peptide-based vaccines by using self-assembled multimeric peptide amphiphiles (PAs). We designed two epitope PAs by conjugating epitope peptides from Enterovirus 71 (EV71) virus particle (VP) 1 and VP3 capsid proteins with different fatty acid chain lengths (VP1PA and VP3PA). These PAs self-assembled into supramolecular structures at a physiological pH, and the resulting structures were characterized using atomic force microscopy. Multi-epitope PAs (m-PAs) consisted of a 1:1 mixture of VP1PA and VP3PA solutions. To evaluate immunogenicity, m-PA constructs were injected with adjuvant subcutaneously into female Balb/c mice. Levels of antigen-specific immunoglobulin G (IgG) and IgG1 in m-PA-injected mice serum samples were analyzed using ELISA and Western blotting. Additionally, cytokine production stimulated by each antigen was measured in splenocytes cultured from immunized mice groups. We found that m-PA showed improved humoral and cellular immune responses compared to the control and peptide groups. The sera from m-PA immunized mice group could neutralize EV71 infection and protect host cells. Thus, self-assembled m-PAs can promote a protective immune response and can be developed as a potential platform technology to produce peptide vaccines against infectious viral diseases. Full article
(This article belongs to the Special Issue Protein Nanostructures for Biomedical Applications)
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13 pages, 3266 KiB  
Article
Bioelectrocatalysis of Hemoglobin on Electrodeposited Ag Nanoflowers toward H2O2 Detection
by Ajay Kumar Yagati, Hien T. Ngoc Le and Sungbo Cho
Nanomaterials 2020, 10(9), 1628; https://doi.org/10.3390/nano10091628 - 19 Aug 2020
Cited by 14 | Viewed by 3190
Abstract
Hydrogen peroxide (H2O2) is a partially reduced metabolite of oxygen that exerts a diverse array of physiological and pathological activities in living organisms. Therefore, the accurate quantitative determination of H2O2 is crucial in clinical diagnostics, the [...] Read more.
Hydrogen peroxide (H2O2) is a partially reduced metabolite of oxygen that exerts a diverse array of physiological and pathological activities in living organisms. Therefore, the accurate quantitative determination of H2O2 is crucial in clinical diagnostics, the food industry, and environmental monitoring. Herein we report the electrosynthesis of silver nanoflowers (AgNFs) on indium tin oxide (ITO) electrodes for direct electron transfer of hemoglobin (Hb) toward the selective quantification of H2O2. After well-ordered and fully-grown AgNFs were created on an ITO substrate by electrodeposition, their morphological and optical properties were analyzed with scanning electron microscopy and UV–Vis spectroscopy. Hb was immobilized on 3-mercaptopropionic acid-coated AgNFs through carbodiimide cross-linking to form an Hb/AgNF/ITO biosensor. Electrochemical measurement and analysis demonstrated that Hb retained its direct electron transfer and electrocatalytic properties and acted as a H2O2 sensor with a detection limit of 0.12 µM and a linear detection range of 0.2 to 3.4 mM in phosphate-buffered saline (PBS). The sensitivity, detection limit, and detection range of the Hb/AgNF/ITO biosensor toward detection H2O2 in human serum was also found to be 0.730 mA mM−1 cm−2, 90 µM, and 0.2 to 2.6 mM, indicating the clinical application for the H2O2 detection of the Hb/AgNF/ITO biosensor. Moreover, interference experiments revealed that the Hb/AgNF/ITO sensor displayed excellent selectivity for H2O2. Full article
(This article belongs to the Special Issue Protein Nanostructures for Biomedical Applications)
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10 pages, 2202 KiB  
Article
Plasticised Regenerated Silk/Gold Nanorods Hybrids as Sealant and Bio-Piezoelectric Materials
by Silvia Bittolo Bon, Michele Rapi, Riccardo Coletta, Antonino Morabito and Luca Valentini
Nanomaterials 2020, 10(1), 179; https://doi.org/10.3390/nano10010179 - 20 Jan 2020
Cited by 12 | Viewed by 3669
Abstract
Manual and mechanical suturing are currently the gold standard for bowel anastomosis. If tissue approximation fails, anastomotic leaks occur. Anastomotic leaks may have catastrophic consequences. The development of a fully absorbable, biocompatible sealant material based on a bio-ink silk fibroin can reduce the [...] Read more.
Manual and mechanical suturing are currently the gold standard for bowel anastomosis. If tissue approximation fails, anastomotic leaks occur. Anastomotic leaks may have catastrophic consequences. The development of a fully absorbable, biocompatible sealant material based on a bio-ink silk fibroin can reduce the chance of anastomotic leaks. We have produced a Ca-modified plasticised regenerated silk (RS) with gold nanorods sealant. This sealant was applied to anastomosed porcine intestine. Water absorption from wet tissue substrate applied compressive strains on hybrid RS films. This compression results in a sealant effect on anastomosis. The increased toughness of the hybrid plasticised RS resulted in the designing of a bio-film with superior elongation at break (i.e., ≈200%) and bursting pressure. We have also reported structure-dependent piezoelectricity of the RS film that shows a piezoelectric effect out of the plane. We hope that in the future, bowel anastomosis can be simplified by providing a multifunctional bio-film that makes feasible the mechanical tissue joint without the need for specific tools and could be used in piezoelectric sealant heads. Full article
(This article belongs to the Special Issue Protein Nanostructures for Biomedical Applications)
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13 pages, 2957 KiB  
Article
Facile and Controllable Fabrication of Protein-Only Nanoparticles through Photo-Induced Crosslinking of Albumin and Their Application as DOX Carriers
by Xiangyu Long, Jun Ren, Chao Zhang, Fangling Ji and Lingyun Jia
Nanomaterials 2019, 9(5), 797; https://doi.org/10.3390/nano9050797 - 24 May 2019
Cited by 5 | Viewed by 4696
Abstract
Protein-based nanoparticles, as an alternative to conventional polymer-based nanoparticles, offer great advantages in biomedical applications owing to their functional and biocompatible characteristics. However, the route of fabrication towards protein-based nanoparticles faces substantial challenges, including limitations in size control and unavoidable usage of toxic [...] Read more.
Protein-based nanoparticles, as an alternative to conventional polymer-based nanoparticles, offer great advantages in biomedical applications owing to their functional and biocompatible characteristics. However, the route of fabrication towards protein-based nanoparticles faces substantial challenges, including limitations in size control and unavoidable usage of toxic crosslinkers or organic solvents, which may raise safety concerns related to products and their degradation components. In the present study, a photo-induced crosslinking approach was developed to prepare stable, size-controlled protein-only nanoparticles. The facile one-step reaction irradiated by visible light enables the formation of monodispersed bovine serum albumin nanoparticles (BSA NPs) within several minutes through a tyrosine photo-redox reaction, requiring no cross-linking agents. The size of the BSA NPs could be precisely manipulated (from 20 to 100 nm) by controlling the duration time of illumination. The resultant BSA NPs exhibited spherical morphology, and the α-helix structure in BSA was preserved. Further study demonstrated that the 35 nm doxorubicin (DOX)-loaded BSA NPs achieved a drug loading content of 6.3%, encapsulation efficiency of 70.7%, and a controlled release profile with responsivity to both pH and reducing conditions. Importantly, the in vitro drug delivery experiment demonstrated efficient cellular internalizations of the DOX-loaded BSA NPs and inhibitory activities on MCF-7 and HeLa cells. This method shows the promise of being a platform for the green synthesis of protein-only nanoparticles for biomedical applications. Full article
(This article belongs to the Special Issue Protein Nanostructures for Biomedical Applications)
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Review

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28 pages, 845 KiB  
Review
Protein Supramolecular Structures: From Self-Assembly to Nanovaccine Design
by Ximena Zottig, Mélanie Côté-Cyr, Dominic Arpin, Denis Archambault and Steve Bourgault
Nanomaterials 2020, 10(5), 1008; https://doi.org/10.3390/nano10051008 - 25 May 2020
Cited by 45 | Viewed by 6411
Abstract
Life-inspired protein supramolecular assemblies have recently attracted considerable attention for the development of next-generation vaccines to fight against infectious diseases, as well as autoimmune diseases and cancer. Protein self-assembly enables atomic scale precision over the final architecture, with a remarkable diversity of structures [...] Read more.
Life-inspired protein supramolecular assemblies have recently attracted considerable attention for the development of next-generation vaccines to fight against infectious diseases, as well as autoimmune diseases and cancer. Protein self-assembly enables atomic scale precision over the final architecture, with a remarkable diversity of structures and functionalities. Self-assembling protein nanovaccines are associated with numerous advantages, including biocompatibility, stability, molecular specificity and multivalency. Owing to their nanoscale size, proteinaceous nature, symmetrical organization and repetitive antigen display, protein assemblies closely mimic most invading pathogens, serving as danger signals for the immune system. Elucidating how the structural and physicochemical properties of the assemblies modulate the potency and the polarization of the immune responses is critical for bottom-up design of vaccines. In this context, this review briefly covers the fundamentals of supramolecular interactions involved in protein self-assembly and presents the strategies to design and functionalize these assemblies. Examples of advanced nanovaccines are presented, and properties of protein supramolecular structures enabling modulation of the immune responses are discussed. Combining the understanding of the self-assembly process at the molecular level with knowledge regarding the activation of the innate and adaptive immune responses will support the design of safe and effective nanovaccines. Full article
(This article belongs to the Special Issue Protein Nanostructures for Biomedical Applications)
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36 pages, 3346 KiB  
Review
Reconfiguring Nature’s Cholesterol Accepting Lipoproteins as Nanoparticle Platforms for Transport and Delivery of Therapeutic and Imaging Agents
by Skylar T. Chuang, Siobanth Cruz and Vasanthy Narayanaswami
Nanomaterials 2020, 10(5), 906; https://doi.org/10.3390/nano10050906 - 8 May 2020
Cited by 20 | Viewed by 4747
Abstract
Apolipoproteins are critical structural and functional components of lipoproteins, which are large supramolecular assemblies composed predominantly of lipids and proteins, and other biomolecules such as nucleic acids. A signature feature of apolipoproteins is the preponderance of amphipathic α-helical motifs that dictate their ability [...] Read more.
Apolipoproteins are critical structural and functional components of lipoproteins, which are large supramolecular assemblies composed predominantly of lipids and proteins, and other biomolecules such as nucleic acids. A signature feature of apolipoproteins is the preponderance of amphipathic α-helical motifs that dictate their ability to make extensive non-covalent inter- or intra-molecular helix–helix interactions in lipid-free states or helix–lipid interactions with hydrophobic biomolecules in lipid-associated states. This review focuses on the latter ability of apolipoproteins, which has been capitalized on to reconstitute synthetic nanoscale binary/ternary lipoprotein complexes composed of apolipoproteins/peptides and lipids that mimic native high-density lipoproteins (HDLs) with the goal to transport drugs. It traces the historical development of our understanding of these nanostructures and how the cholesterol accepting property of HDL has been reconfigured to develop them as drug-loading platforms. The review provides the structural perspective of these platforms with different types of apolipoproteins and an overview of their synthesis. It also examines the cargo that have been loaded into the core for therapeutic and imaging purposes. Finally, it lays out the merits and challenges associated with apolipoprotein-based nanostructures with a future perspective calling for a need to develop “zip-code”-based delivery for therapeutic and diagnostic applications. Full article
(This article belongs to the Special Issue Protein Nanostructures for Biomedical Applications)
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20 pages, 2737 KiB  
Review
Systemically Administered, Target-Specific, Multi-Functional Therapeutic Recombinant Proteins in Regenerative Medicine
by Tero A.H. Järvinen and Toini Pemmari
Nanomaterials 2020, 10(2), 226; https://doi.org/10.3390/nano10020226 - 28 Jan 2020
Cited by 12 | Viewed by 4539
Abstract
Growth factors, chemokines and cytokines guide tissue regeneration after injuries. However, their applications as recombinant proteins are almost non-existent due to the difficulty of maintaining their bioactivity in the protease-rich milieu of injured tissues in humans. Safety concerns have ruled out their systemic [...] Read more.
Growth factors, chemokines and cytokines guide tissue regeneration after injuries. However, their applications as recombinant proteins are almost non-existent due to the difficulty of maintaining their bioactivity in the protease-rich milieu of injured tissues in humans. Safety concerns have ruled out their systemic administration. The vascular system provides a natural platform for circumvent the limitations of the local delivery of protein-based therapeutics. Tissue selectivity in drug accumulation can be obtained as organ-specific molecular signatures exist in the blood vessels in each tissue, essentially forming a postal code system (“vascular zip codes”) within the vasculature. These target-specific “vascular zip codes” can be exploited in regenerative medicine as the angiogenic blood vessels in the regenerating tissues have a unique molecular signature. The identification of vascular homing peptides capable of finding these unique “vascular zip codes” after their systemic administration provides an appealing opportunity for the target-specific delivery of therapeutics to tissue injuries. Therapeutic proteins can be “packaged” together with homing peptides by expressing them as multi-functional recombinant proteins. These multi-functional recombinant proteins provide an example how molecular engineering gives to a compound an ability to home to regenerating tissue and enhance its therapeutic potential. Regenerative medicine has been dominated by the locally applied therapeutic approaches despite these therapies are not moving to clinical medicine with success. There might be a time to change the paradigm towards systemically administered, target organ-specific therapeutic molecules in future drug discovery and development for regenerative medicine. Full article
(This article belongs to the Special Issue Protein Nanostructures for Biomedical Applications)
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