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Pharmaceutical Nanotechnology

Editor-in-Chief

ISSN (Print): 2211-7385
ISSN (Online): 2211-7393

Mini-Review Article

Protein-Based Drug Delivery Nanomedicine Platforms: Recent Developments

Author(s): Alaa A.A. Aljabali*, Meriem Rezigue, Rawan H. Alsharedeh, Mohammad A. Obeid, Vijay Mishra, Ángel Serrano-Aroca and Murtaza M. Tambuwala

Volume 10, Issue 4, 2022

Published on: 07 October, 2022

Page: [257 - 267] Pages: 11

DOI: 10.2174/2211738510666220817120307

Price: $65

Abstract

Background: Naturally occurring protein cages, both viral and non-viral assemblies, have been developed for various pharmaceutical applications. Protein cages are ideal platforms as they are compatible, biodegradable, bioavailable, and amenable to chemical and genetic modification to impart new functionalities for selective targeting or tracking of proteins. The ferritin/ apoferritin protein cage, plant-derived viral capsids, the small Heat shock protein, albumin, soy and whey protein, collagen, and gelatin have all been exploited and characterized as drugdelivery vehicles. Protein cages come in many shapes and types with unique features such as unmatched uniformity, size, and conjugations.

Objectives: The recent strategic development of drug delivery will be covered in this review, emphasizing polymer-based, specifically protein-based, drug delivery nanomedicine platforms. The potential and drawbacks of each kind of protein-based drug-delivery system will also be highlighted.

Methods: Research examining the usability of nanomaterials in the pharmaceutical and medical sectors were identified by employing bibliographic databases and web search engines.

Results: Rings, tubes, and cages are unique protein structures that occur in the biological environment and might serve as building blocks for nanomachines. Furthermore, numerous virions can undergo reversible structural conformational changes that open or close gated pores, allowing customizable accessibility to their core and ideal delivery vehicles.

Conclusion: Protein cages' biocompatibility and their ability to be precisely engineered indicate they have significant potential in drug delivery and intracellular administration.

Keywords: Protein nanoparticles, Nanomedicine, Pharmaceutical nanotechnology, viruses, Drug delivery

Graphical Abstract

[1]
Zhou J, Krishnan N, Jiang Y, Fang RH, Zhang L. Nanotechnology for virus treatment. Nano Today 2021; 36: 101031.
[http://dx.doi.org/10.1016/j.nantod.2020.101031] [PMID: 33519948]
[2]
Aljabali AAA, Obeid MA. Inorganic-organic nanomaterials for therapeutics and molecular imaging applications. Nanosci Nanotechnol Asia 2020; 10(6): 748-65.
[http://dx.doi.org/10.2174/2210681209666190807145229]
[3]
Singh P, Gonzalez MJ, Manchester M. Viruses and their uses in nanotechnology. Drug Dev Res 2006; 67(1): 23-41.
[http://dx.doi.org/10.1002/ddr.20064]
[4]
Tavanti F, Pedone A, Menziani MC. Multiscale molecular dynamics simulation of multiple protein adsorption on gold nanoparticles. Int J Mol Sci 2019; 20(14): 3539.
[http://dx.doi.org/10.3390/ijms20143539] [PMID: 31331044]
[5]
Mahdavi K, Zinatloo-Ajabshir S, Yousif QA, Salavati-Niasari M. Enhanced photocatalytic degradation of toxic contaminants using Dy2O3-SiO2 ceramic nanostructured materials fabricated by a new, simple and rapid sonochemical approach. Ultrason Sonochem 2022; 82: 105892.
[http://dx.doi.org/10.1016/j.ultsonch.2021.105892] [PMID: 34959201]
[6]
Röder J, Dickmeis C, Commandeur U. Small, smaller, nano: New applications for potato virus X in nanotechnology. 2019; 10(158)
[7]
Lua LHL, Connors NK, Sainsbury F, Chuan YP, Wibowo N, Middelberg APJ. Bioengineering virus-like particles as vaccines. Biotechnol Bioeng 2014; 111(3): 425-40.
[http://dx.doi.org/10.1002/bit.25159] [PMID: 24347238]
[8]
Sainsbury F, Saxena P, Aljabali AAA, Saunders K, Evans DJ, Lomonossoff GP. Genetic engineering and characterization of cowpea mosaic virus empty virus-like particles Virus Hybrids as Nanomaterials. Springer 2014; pp. 139-53.
[http://dx.doi.org/10.1007/978-1-62703-751-8_11]
[9]
Aljabali AAA, Alzoubi L, Hamzat Y, et al. A potential MRI agent and an anticancer drug encapsulated within CPMV virus-like particles. Comb Chem High Throughput Screen 2021; 24(10): 1557-71.
[http://dx.doi.org/10.2174/1386207323666200914110012] [PMID: 32928083]
[10]
Aljabali AAA, Barclay JE, Cespedes O, et al. Charge modified Cowpea mosaic virus particles for templated mineralization. Adv Funct Mater 2011; 21(21): 4137-42.
[http://dx.doi.org/10.1002/adfm.201101048]
[11]
Aljabali AAA, Evans DJ. Polyelectrolyte-modified cowpea mosaic virus for the synthesis of gold nanoparticles Virus Hybrids as Nanomaterials. Springer 2014; pp. 97-103.
[http://dx.doi.org/10.1007/978-1-62703-751-8_7]
[12]
Aljabali AAA, Hassan SS, Pabari RM, et al. The viral capsid as novel nanomaterials for drug delivery. Future Sci OA 2021; 7(9): FSO744.
[http://dx.doi.org/10.2144/fsoa-2021-0031] [PMID: 34737885]
[13]
Jaafar M, Aljabali AAA, Berlanga I, et al. Structural insights into magnetic clusters grown inside virus capsids. ACS Appl Mater Interfaces 2014; 6(23): 20936-42.
[http://dx.doi.org/10.1021/am505682x] [PMID: 25405995]
[14]
Alaa AA, Aljabali J, Barclay E, et al. Redox-active ferrocene-modified Cowpea mosaic virus nanoparticles. Dalton Trans 2010; 39: 7569.
[http://dx.doi.org/10.1039/c0dt00495b]
[15]
Vishnu VGP, Hema M, Sushmitha C, Savithri HS, Natraj U, Murthy MRN. Development of sesbania mosaic virus nanoparticles for imaging. Arch Virol 2019; 164(2): 497-507.
[http://dx.doi.org/10.1007/s00705-018-4097-y] [PMID: 30430265]
[16]
Shoeb E, Hefferon K. Future of cancer immunotherapy using plant virus-based nanoparticles. Future Sci OA 2019; 5(7): FSO401.
[http://dx.doi.org/10.2144/fsoa-2019-0001] [PMID: 31428448]
[17]
Pitek AS, Hu H, Shukla S, Steinmetz NF. Cancer theranostic applications of albumin-coated tobacco mosaic virus nanoparticles. ACS Appl Mater Interfaces 2018; 10(46): 39468-77.
[http://dx.doi.org/10.1021/acsami.8b12499] [PMID: 30403330]
[18]
Hema M, Vardhan GV, Savithri HS, Murthy MRN. Emerging trends in the development of plant virus-based nanoparticles and their biomedical applications. Recent Developments in Applied Microbiology and Biochemistry. Academic Press 2019; pp. 61-82.
[19]
Bhushan B, Kumar SU, Matai I, Sachdev A, Dubey P, Gopinath P. Ferritin nanocages: A novel platform for biomedical applications. J Biomed Nanotechnol 2014; 10(10): 2950-76.
[http://dx.doi.org/10.1166/jbn.2014.1980] [PMID: 25992425]
[20]
Truffi M, Fiandra L, Sorrentino L, Monieri M, Corsi F, Mazzucchelli S. Ferritin nanocages: A biological platform for drug delivery, imaging and theranostics in cancer. Pharmacol Res 2016; 107: 57-65.
[http://dx.doi.org/10.1016/j.phrs.2016.03.002] [PMID: 26968122]
[21]
Daniels TR, Delgado T, Rodriguez JA, Helguera G, Penichet ML. The transferrin receptor part I: Biology and targeting with cytotoxic antibodies for the treatment of cancer. Clin Immunol 2006; 121(2): 144-58.
[http://dx.doi.org/10.1016/j.clim.2006.06.010] [PMID: 16904380]
[22]
Liang M, Fan K, Zhou M, et al. H-ferritin-nanocaged doxorubicin nanoparticles specifically target and kill tumors with a single-dose injection. Proc Natl Acad Sci USA 2014; 111(41): 14900-5.
[http://dx.doi.org/10.1073/pnas.1407808111] [PMID: 25267615]
[23]
Falvo E, Malagrinò F, Arcovito A, et al. The presence of glutamate residues on the PAS sequence of the stimuli-sensitive nano-ferritin improves in vivo biodistribution and mitoxantrone encapsulation homogeneity. J Cont Release 2018; 275: 177-85.
[24]
Sun X, Hong Y, Gong Y, Zheng S, Xie D. Bioengineered ferritin nanocarriers for cancer therapy. Int J Mol Sci 2021; 22(13): 7023.
[http://dx.doi.org/10.3390/ijms22137023] [PMID: 34209892]
[25]
Powell JJ, Bruggraber SF, Faria N, et al. A nano-disperse ferritin-core mimetic that efficiently corrects anemia without luminal iron redox activity. Nanomedicine 2014; 10(7): 1529-38.
[http://dx.doi.org/10.1016/j.nano.2013.12.011] [PMID: 24394211]
[26]
Han JA, Kang YJ, Shin C, et al. Ferritin protein cage nanoparticles as versatile antigen delivery nanoplatforms for dendritic cell (DC)-based vaccine development. Nanomedicine 2014; 10(3): 561-9.
[http://dx.doi.org/10.1016/j.nano.2013.11.003] [PMID: 24262997]
[27]
Zhen Z, Tang W, Chen H, et al. RGD-modified apoferritin nanoparticles for efficient drug delivery to tumors. ACS Nano 2013; 7(6): 4830-7.
[http://dx.doi.org/10.1021/nn305791q] [PMID: 23718215]
[28]
Lei Y, Hamada Y, Li J, et al. Targeted tumor delivery and controlled release of neuronal drugs with ferritin nanoparticles to regulate pancreatic cancer progression. J Control Release 2016; 232: 131-42.
[29]
Zeltins A. Construction and characterization of virus-like particles. A review. Mol Biotechnol 2013; 53(1): 92-107.
[http://dx.doi.org/10.1007/s12033-012-9598-4] [PMID: 23001867]
[30]
Kuruppu AI, Zhang L, Collins H, Turyanska L, Thomas NR, Bradshaw TD. An apoferritin-based drug delivery system for the tyrosine kinase inhibitor gefitinib. Adv Healthc Mater 2015; 4(18): 2816-21.
[http://dx.doi.org/10.1002/adhm.201500389] [PMID: 26592186]
[31]
Walcher L, Kistenmacher AK, Suo H, et al. Cancer stem cells-origins and biomarkers: Perspectives for targeted personalized therapies. Front Immunol 2020; 11: 1280.
[http://dx.doi.org/10.3389/fimmu.2020.01280] [PMID: 32849491]
[32]
Fracasso G, Falvo E, Colotti G, et al. Selective delivery of doxorubicin by novel stimuli-sensitive nano-ferritins overcomes tumor refractoriness. J Control Release 2016; 239: 10-8.
[33]
Lee EJ, Lee SJ, Kang YS, et al. Engineered proteinticles for targeted delivery of siRNA to cancer cells. Adv Funct Mater 2015; 25(8): 1279-86.
[http://dx.doi.org/10.1002/adfm.201403680]
[34]
Jiang B, Zhang R, Zhang J, et al. GRP78-targeted ferritin nanocaged ultra-high dose of doxorubicin for hepatocellular carcinoma therapy. Theranostics 2019; 9(8): 2167-82.
[http://dx.doi.org/10.7150/thno.30867] [PMID: 31149036]
[35]
Zhai M, Wang Y, Zhang L, et al. Glioma targeting peptide modified apoferritin nanocage. Drug Deliv 2018; 25(1): 1013-24.
[http://dx.doi.org/10.1080/10717544.2018.1464082] [PMID: 29726297]
[36]
Zhang J, Zeng Y, Su M, et al. Multifunctional ferritin nanoparticles as theranostics for imaging-guided tumor phototherapy. J Biomed Nanotechnol 2019; 15(7): 1546-55.
[http://dx.doi.org/10.1166/jbn.2019.2788] [PMID: 31196357]
[37]
Isaacs JS, Xu W, Neckers L. Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 2003; 3(3): 213-7.
[38]
Kim KK, Kim R, Kim SH. Crystal structure of a small heat-shock protein. Nature 1998; 394(6693): 595-9.
[http://dx.doi.org/10.1038/29106] [PMID: 9707123]
[39]
Li Z-W, Li X, Yu Q-Y, Xiang Z-H, Kishino H, Zhang Z. The small heat shock protein (sHSP) genes in the silkworm, Bombyx mori, and comparative analysis with other insect sHSP genes. BMC Evol Biol 2009; 9(1): 215.
[http://dx.doi.org/10.1186/1471-2148-9-215] [PMID: 19715580]
[40]
Toita R, Murata M, Tabata S, et al. Development of human hepatocellular carcinoma cell-targeted protein cages. Bioconjug Chem 2012; 23(7): 1494-501.
[http://dx.doi.org/10.1021/bc300015f] [PMID: 22621213]
[41]
Park TS, Kim HR, Koh JS, et al. Heat shock protein 70 as a predictive marker for platinum-based adjuvant chemotherapy in patients with resected non-small cell lung cancer. Lung Cancer 2014; 86(2): 262-7.
[http://dx.doi.org/10.1016/j.lungcan.2014.08.009] [PMID: 25261232]
[42]
Flenniken ML, Willits DA, Harmsen AL, et al. Melanoma and lymphocyte cell-specific targeting incorporated into a heat shock protein cage architecture. Chem Biol 2006; 13(2): 161-70.
[http://dx.doi.org/10.1016/j.chembiol.2005.11.007] [PMID: 16492564]
[43]
Murata M, Narahara S, Umezaki K, et al. Liver cell specific targeting by the preS1 domain of hepatitis B virus surface antigen displayed on protein nanocages. Int J Nanomedicine 2012; 7: 4353-62.
[http://dx.doi.org/10.2147/IJN.S31365] [PMID: 22927755]
[44]
Dash S, Rao KV, Panda SK. Receptor for pre-S1(21-47) component of hepatitis B virus on the liver cell: Role in virus cell interaction. J Med Virol 1992; 37(2): 116-21.
[http://dx.doi.org/10.1002/jmv.1890370208] [PMID: 1629710]
[45]
Snijder J, Kononova O, Barbu IM, et al. Assembly and mechanical properties of the cargo-free and cargo-loaded bacterial nanocompartment encapsulin. Biomacromolecules 2016; 17(8): 2522-9.
[http://dx.doi.org/10.1021/acs.biomac.6b00469] [PMID: 27355101]
[46]
Gabashvili AN, Chmelyuk NS, Efremova MV, Malinovskaya JA, Semkina AS, Abakumov MA. Encapsulins-bacterial protein nanocompartments: Structure, properties, and application. Biomolecules 2020; 10(6): E966.
[http://dx.doi.org/10.3390/biom10060966] [PMID: 32604934]
[47]
Rurup WF, Snijder J, Koay MS, Heck AJ, Cornelissen JJ. Self-sorting of foreign proteins in a bacterial nanocompartment. J Am Chem Soc 2014; 136(10): 3828-32.
[http://dx.doi.org/10.1021/ja410891c] [PMID: 24527660]
[48]
He D, Hughes S, Vanden-Hehir S, et al. Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments. eLife 2016; 5: 5.
[http://dx.doi.org/10.7554/eLife.18972] [PMID: 27529188]
[49]
Benner NL, Zang X, Buehler DC, et al. Vault nanoparticles: Chemical modifications for imaging and enhanced delivery. ACS Nano 2017; 11(1): 872-81.
[http://dx.doi.org/10.1021/acsnano.6b07440] [PMID: 28029784]
[50]
Kedersha NL, Heuser JE, Chugani DC, Rome LH, Vaults III, Vaults III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry. J Cell Biol 1991; 112(2): 225-35.
[http://dx.doi.org/10.1083/jcb.112.2.225] [PMID: 1988458]
[51]
Tanaka H, Tsukihara T. Structural studies of large nucleoprotein particles, vaults. Proc Jpn Acad, Ser B, Phys Biol Sci 2012; 88(8): 416-33.
[http://dx.doi.org/10.2183/pjab.88.416] [PMID: 23060231]
[52]
Kickhoefer VA, Siva AC, Kedersha NL, et al. The 193-kD vault protein, VPARP, is a novel poly(ADP-ribose) polymerase. J Cell Biol 1999; 146(5): 917-28.
[http://dx.doi.org/10.1083/jcb.146.5.917] [PMID: 10477748]
[53]
Matsumoto NM, Buchman GW, Rome LH, Maynard HD. Dual pH-and temperature-responsive protein nanoparticles. Eur Polym J 2015; 69: 532-9.
[http://dx.doi.org/10.1016/j.eurpolymj.2015.01.043] [PMID: 26365998]
[54]
Poderycki MJ, Kickhoefer VA, Kaddis CS, et al. The vault exterior shell is a dynamic structure that allows incorporation of vault-associated proteins into its interior. Biochemistry 2006; 45(39): 12184-93.
[http://dx.doi.org/10.1021/bi0610552] [PMID: 17002318]
[55]
Ding K, Zhang X, Mrazek J, et al. Solution structures of engineered vault particles. Structure 2018; 26(4): 619-23.
[56]
Esfandiary R, Kickhoefer VA, Rome LH, Joshi SB, Middaugh CR. Structural stability of vault particles. J Pharm Sci 2009; 98(4): 1376-86.
[http://dx.doi.org/10.1002/jps.21508] [PMID: 18683860]
[57]
Llauró A, Guerra P, Kant R, Bothner B, Verdaguer N, de Pablo PJ. Decrease in pH destabilizes individual vault nanocages by weakening the inter-protein lateral interaction. Sci Rep 2016; 6(1): 34143.
[http://dx.doi.org/10.1038/srep34143] [PMID: 27739422]
[58]
Mikyas Y, Makabi M, Raval-Fernandes S, et al. Cryoelectron microscopy imaging of recombinant and tissue derived vaults: Localization of the MVP N termini and VPARP. J Mol Biol 2004; 344(1): 91-105.
[http://dx.doi.org/10.1016/j.jmb.2004.09.021] [PMID: 15504404]
[59]
Han M, Kickhoefer VA, Nemerow GR, Rome LH. Targeted vault nanoparticles engineered with an endosomolytic peptide deliver biomolecules to the cytoplasm. ACS Nano 2011; 5(8): 6128-37.
[http://dx.doi.org/10.1021/nn2014613] [PMID: 21740042]
[60]
Buehler DC, Toso DB, Kickhoefer VA, Zhou ZH, Rome LH. Vaults engineered for hydrophobic drug delivery. Small 2011; 7(10): 1432-9.
[http://dx.doi.org/10.1002/smll.201002274] [PMID: 21506266]
[61]
Muñoz-Juan A, Carreño A, Mendoza R, Corchero JL. Latest advances in the development of eukaryotic vaults as targeted drug delivery systems. Pharmaceutics 2019; 11(7): E300.
[http://dx.doi.org/10.3390/pharmaceutics11070300] [PMID: 31261673]
[62]
Nolz JC, Starbeck-Miller GR, Harty JT. Naive, effector and memory CD8 T-cell trafficking: Parallels and distinctions. Immunotherapy 2011; 3(10): 1223-33.
[http://dx.doi.org/10.2217/imt.11.100] [PMID: 21995573]
[63]
Endo M, de Graaff MA, Ingram DR, et al. NY-ESO-1 (CTAG1B) expression in mesenchymal tumors. Mod Pathol 2015; 28(4): 587-95.
[http://dx.doi.org/10.1038/modpathol.2014.155] [PMID: 25412843]
[64]
Zhu Y, Jiang J, Said-Sadier N, et al. Activation of the NLRP3 inflammasome by vault nanoparticles expressing a chlamydial epitope. Vaccine 2015; 33(2): 298-306.
[http://dx.doi.org/10.1016/j.vaccine.2014.11.028] [PMID: 25448112]
[65]
Sleep D. Albumin and its application in drug delivery. Expert Opin Drug Deliv 2015; 12(5): 793-812.
[http://dx.doi.org/10.1517/17425247.2015.993313] [PMID: 25518870]
[66]
Elzoghby AO, Samy WM, Elgindy NA. Protein-based nanocarriers as promising drug and gene delivery systems. J Control Release 2012; 161(1): 38-49.
[http://dx.doi.org/10.1016/j.jconrel.2012.04.036] [PMID: 22564368]
[67]
Maham A, Tang Z, Wu H, Wang J, Lin Y. Protein-based nanomedicine platforms for drug delivery. Small 2009; 5(15): 1706-21.
[http://dx.doi.org/10.1002/smll.200801602] [PMID: 19572330]
[68]
Jahanshahi M, Sanati MH, Babaei Z. Optimization of parameters for the fabrication of gelatin nanoparticles by the Taguchi robust design method. J Appl Stat 2008; 35(12): 1345-53.
[http://dx.doi.org/10.1080/02664760802382426]
[69]
Qazvini NT, Zinatloo S. Synthesis and characterization of gelatin nanoparticles using CDI/NHS as a non-toxic cross-linking system. J Mater Sci Mater Med 2011; 22(1): 63-9.
[http://dx.doi.org/10.1007/s10856-010-4178-2] [PMID: 21052793]
[70]
Zinatloo AS, Taheri QN. Effect of some synthetic parameters on size and polydispersity index of gelatin nanoparticles cross-linked by CDI/NHS system. J Nanostructures 2015; 5(2): 137-44.
[71]
Zinatloo-Ajabshir Z, Zinatloo-Ajabshir S. Preparation and characterization of curcumin niosomal nanoparticles via a simple and ecofriendly route. J Nanostructures 2019; 9(4): 784-90.
[72]
Lohcharoenkal W, Wang L, Chen YC, Rojanasakul Y. Protein nanoparticles as drug delivery carriers for cancer therapy. BioMed Res Int 2014; 2014: 180549.
[http://dx.doi.org/10.1155/2014/180549]
[73]
Bakshi HA, Zoubi MSA, Hakkim FL, et al. Dietary crocin is protective in pancreatic cancer while reducing radiation-induced hepatic oxidative damage. Nutrients 2020; 12(6): E1901.
[http://dx.doi.org/10.3390/nu12061901] [PMID: 32604971]

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