Nanoparticles in Medicine [1st ed. 2020] 978-981-13-8953-5, 978-981-13-8954-2

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Nanoparticles in Medicine [1st ed. 2020]
 978-981-13-8953-5, 978-981-13-8954-2

Table of contents :
Front Matter ....Pages i-xi
Theranostic Applications of Lysozyme-Based Nanoparticles (Sourav Das, Manideep Pabba, M. E. Dhushyandhun, Chitta Ranjan Patra)....Pages 1-23
Emerging Nanomaterials for Cancer Therapy (Sanjay Kumar, Pratibha Kumari, Rajeev Singh)....Pages 25-54
Application of Nanoparticles in Dentistry: Current Trends (Subhashree Priyadarsini, Sumit Mukherjee, Janmejaya Bag, Nibedita Nayak, Monalisa Mishra)....Pages 55-98
Microbial Synthesis of Silver Nanoparticles and Their Biological Potential (Annuja Anandaradje, Vadivel Meyappan, Indramani Kumar, Natarajan Sakthivel)....Pages 99-133
Fluoride Nanoparticles for Biomedical Applications (M. S. Pudovkin, R. M. Rakhmatullin)....Pages 135-174
Gold Nanostructures in Medicine and Biology (Siavash Iravani, Ghazaleh Jamalipour Soufi)....Pages 175-183
Fungus-Mediated Nanoparticles: Characterization and Biomedical Advances (S. Rajeshkumar, D. Sivapriya)....Pages 185-199
Precautions to Avoid Consequences Leading to Nanotoxification (Sharda Sundaram Sanjay)....Pages 201-220

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Nanoparticles in Medicine Ashutosh Kumar Shukla  Editor

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Nanoparticles in Medicine

Ashutosh Kumar Shukla Editor

Nanoparticles in Medicine

Editor Ashutosh Kumar Shukla Physics Department, Ewing Christian College University of Allahabad Allahabad, Uttar Pradesh India

ISBN 978-981-13-8953-5    ISBN 978-981-13-8954-2 (eBook) https://doi.org/10.1007/978-981-13-8954-2 © Springer Nature Singapore Pte Ltd. 2020 This work is subject to copyright. All rights are reserved by the Publisher, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilms or in any other physical way, and transmission or information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed. The use of general descriptive names, registered names, trademarks, service marks, etc. in this publication does not imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws and regulations and therefore free for general use. The publisher, the authors, and the editors are safe to assume that the advice and information in this book are believed to be true and accurate at the date of publication. Neither the publisher nor the authors or the editors give a warranty, expressed or implied, with respect to the material contained herein or for any errors or omissions that may have been made. The publisher remains neutral with regard to jurisdictional claims in published maps and institutional affiliations. This Springer imprint is published by the registered company Springer Nature Singapore Pte Ltd. The registered company address is: 152 Beach Road, #21-01/04 Gateway East, Singapore 189721, Singapore

To my parents.

Preface

This collection intends to highlight the potential applications of nanoparticles in medicine. Gold and silver nanoparticles, rare earth-doped fluoride nanoparticles, protein-based nanoparticles, and fungal-mediated nanoparticles have been covered in different chapters. The applications in different fields of medicine covered in this volume include cancer therapy, photodynamic therapy, antioxidant therapy, dentistry, and caries prevention. Related toxicity issues have been addressed in individual chapters and in a separate chapter as well. I am thankful to the expert contributors for contributing to this volume. My special thanks to Prof. Alex I. Smirnov, Department of Chemistry, North Carolina State University, USA; Prof. Anjana Pandey, Department of Biotechnology, MNNIT, Allahabad; Dr. Chitta Ranjan Patra, Department of Applied Biology, CSIR-IICT, Hyderabad; Dr. Monalisa Mishra, Department of Life Science, NIT, Rourkela; and Dr. S Rajeshkumar, Department of Pharmacology, Saveetha Dental College, Chennai, who kindly reviewed the manuscripts for this volume. I sincerely thank Dr. Naren Aggarwal, Executive Editor, Clinical Medicine, Springer (India) Private Limited, for giving me the opportunity to present this book to the readers. I also thank Teena Bedi, Associate Editor, Clinical Medicine, Springer (India) Private Limited, and Mr. Ejaz Ahmad, Project Coordinator (Books), for their support during the publication process. It was a good learning experience for me to go through individual chapters and hope that it will be a good experience for the audience too. Allahabad, India May 2019

Ashutosh Kumar Shukla

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Contents

1 Theranostic Applications of Lysozyme-­Based Nanoparticles������������������   1 Sourav Das, Manideep Pabba, M. E. Dhushyandhun, and Chitta Ranjan Patra 2 Emerging Nanomaterials for Cancer Therapy������������������������������������������  25 Sanjay Kumar, Pratibha Kumari, and Rajeev Singh 3 Application of Nanoparticles in Dentistry: Current Trends��������������������  55 Subhashree Priyadarsini, Sumit Mukherjee, Janmejaya Bag, Nibedita Nayak, and Monalisa Mishra 4 Microbial Synthesis of Silver Nanoparticles and Their Biological Potential��������������������������������������������������������������������  99 Annuja Anandaradje, Vadivel Meyappan, Indramani Kumar, and Natarajan Sakthivel 5 Fluoride Nanoparticles for Biomedical Applications�������������������������������� 135 M. S. Pudovkin and R. M. Rakhmatullin 6 Gold Nanostructures in Medicine and Biology ���������������������������������������� 175 Siavash Iravani and Ghazaleh Jamalipour Soufi 7 Fungus-Mediated Nanoparticles: Characterization and Biomedical Advances���������������������������������������������������������������������������� 185 S. Rajeshkumar and D. Sivapriya 8 Precautions to Avoid Consequences Leading to Nanotoxification���������� 201 Sharda Sundaram Sanjay

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About the Editor

Ashutosh  Kumar  Shukla  holds B.Sc., M.Sc., and D.  Phil. degrees from the University of Allahabad. His doctoral research involved using electron spin resonance spectroscopy and optical absorption spectroscopy to investigate transition ion-doped single crystals. He has been a university teacher and researcher for 17  years and is currently an Associate Professor of Physics at Ewing Christian College, Allahabad, a University of Allahabad institution. He also served as an Associate Professor (Pure and Applied Physics) at Guru Ghasidas Vishwavidyalaya, Bilaspur, C.G. (a central university). Dr. Shukla has successfully completed research projects in the area of electron spin resonance, funded by the University Grants Commission, India’s main higher education body. He has presented his research at various international events in countries including the USA, UK, Germany, Spain, and Russia. He has published a number of research papers in peer-reviewed journals and has edited numerous volumes. He has delivered several invited lectures on characterization techniques at national and international conferences and workshops. He also reviews manuscripts for a number of international journals. He has received many scholarships and fellowships, including a National Scholarship; Government of U. P. Ministry of Higher Education Scholarship; and research fellowships from the Council of Science & Technology, Lucknow; Council of Scientific & Industrial Research, New Delhi; and the Indian National Science Academy-Bilateral Exchange Fellowship.

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Theranostic Applications of Lysozyme-­ Based Nanoparticles Sourav Das, Manideep Pabba, M. E. Dhushyandhun, and Chitta Ranjan Patra

Abbreviations A549 Adenocarcinomic human alveolar basal epithelial cells ABTS 2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) AgNPs Silver nanoparticles AuNCs Lysozyme-gold nanocluster CD Circular dichroism CF Cystic fibrosis CMC Critical micelle concentrations COPD Chronic obstructive pulmonary diseases CuNCs Copper nanocluster EDTA Ethylenediaminetetraacetic acid EGF Epidermal growth factor FRET Forster non-radiative energy transfer FT-IR Fourier-transform infrared spectroscopy HeLa Cervical cancer cells (human) HGT Horizontal gene transfer hLYS Human lysozyme HPLC High-performance liquid chromatography LOD Lowest detection limit LYMB Lysozyme microbubble S. Das · C. R. Patra (*) Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, Uttar Pradesh, India Department of Applied Biology, CSIR-Indian Institute of Chemical Technology, Hyderabad, Telangana, India e-mail: [email protected] M. Pabba · M. E. Dhushyandhun Department of Applied Biology, CSIR-Indian Institute of Chemical Technology, Hyderabad, Telangana, India © Springer Nature Singapore Pte Ltd. 2020 A. K. Shukla (ed.), Nanoparticles in Medicine, https://doi.org/10.1007/978-981-13-8954-2_1

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MALDI Matrix-assisted laser desorption/ionization MCF-7 Michigan cancer foundation-7 MD Molecular dynamics MIC Minimum inhibitory concentration NAG-3 N-acetyl-d-glucosamine NC Nanoclusters ND Nanodiamonds NHF Normal human foreskin fibroblast NP Nanoparticles PBS Phosphate buffered saline PDRAB Pan-drug resistant Acinetobacter baumannii PEI Polyethyleneimine rHlys Recombinant human lysozyme ROS Reactive oxygen species SAP Serum amyloid p component SDS Sodium dodecyl sulfate snLYZ Self-assembled nanostructured lysozyme TDD Transdermal drug delivery THB Theobromine THP Theophylline TMB 3,3′,5,5′-Tetramethylbenzidine US Ultrasound VRE Vancomycin-resistant Enterococcus faecalis WT Wild type XRD X-ray crystallography XTT 2,3-Bis-(2-methoxy-4-nitro5-sulfophenyl)-2H-tetrazolium-5-­ carboxanilide salt

1.1

Introduction

Lysozyme is an enzyme (anti-bacterial) generally distributed in divergent biological fluids, tissues as well as in animal secretions (Callewaert and Michiels 2010). It has various important applications such as anti-bacterial, anti-inflammatory, and anti-­ proliferative activities (Salton 1957; Ye et al. 2008). Recent reports demonstrate that the importance of this small globular protein relies on its substantial use as a model protein in order to know the structure, dynamics, function as well as folding of the proteins (mainly the underlying principle) (Sonu et  al. 2016). The high natural abundance of this protein leads to the development of various nanoparticles reflecting its broad spectrum of usage. Lysozyme was first discovered in the year of 1909. But, this protein was first recognized by Alexander Fleming in the year of 1922 who coined it as “Lysozyme” (Fleming and Wright Almroth 1922). Now-a-days, nanotechnology has been extensively used in the various areas of science and technology. The emergence of the nanotechnology in the field of biotechnology leads to the development of new kind of nanoparticles. Meanwhile, due to several advantages

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and lesser toxicity profile, the protein-based nanoparticles have got the remarkable importance (Tarhini et al. 2017). Recently, scientists are relentlessly making various kinds of protein-based nanoparticles especially lysozyme proteins useful for numerous applications such as drug delivery, imaging, and sensing. In addition, the uniquely faceted tunable structure of the protein lysozyme made it useful in making various nanoparticles including inorganic metals like gold, silver, platinum, silica, copper, and iron (Ghosh et al. 2014; Li et al. 2017). Furthermore, the most recent advances move toward the development of new treatment strategies using these protein-based nanoparticles. Herein, this chapter will mainstay on the theranostic applications of lysozyme-based nanoparticles and the interactions between lysozyme and the metal nanoparticles. Finally, this chapter will provide a brief overview on the properties of lysozyme as well as its applications in a concise manner.

1.1.1 Lysozyme and Its Background Lysozyme is a ubiquitous anti-microbial enzyme generally found in fluids, secretions such as human saliva, milk, tears, even all mucosal surfaces, respiratory tract, and digestive tract. It is also available in both animals and plants (e.g., papaya latex) (Murakami et al. 1998; Peeters and Vantrappen 1975). Lysozyme has high thermal stability having melting point 72 °C (at pH 5.0) and quite stable at higher pH range. The iso-electric point of this protein is 11.35. According to the reports, in egg white large amount of lysozyme can be found (Venkataramani et  al. 2013). Lysozyme (14.3 KDa) has 129 amino acids with four cysteine residues. It sustains the condensed globular structure with an active site at the protein surface in physiological condition. Deep down the complicated secondary structure, it has five helical regions along with the alpha helices, beta sheet, random coil, and beta turns. According to reports, the crystal form of this protein can be obtained by binding the trisaccharide (NAG-3: N-acetyl-d-glucosamine) in its substrate groove (Russell et al. 2017). It has been observed from the crystallographic analysis that the lysozyme (obtained from chicken egg) has high amount of arginine and has no sulfhydryl group. Generally, it demonstrates two conformations, active site (open) and inactive site (closed) which change accordingly during the moment of action (Choi et al. 2012). The basic properties of the lysozyme helps in forming the complexes with negatively charged substances (Salton 1957).

1.1.2 Biological Activity Lysozyme shows  catalyzing activity by hydrolyzing the peptidoglycan residues such as 1,4-beta-linkages between N-acetyl-d-glucosamine and N-acetylmuramic acid found in bacterial cell wall (Scanlon et al. 2010). Peptidoglycan which is one of the primary components of the bacterial cell wall delivers resistance against turgor pressure. Therefore, lysozyme builds a kind of first line defense mechanism against bacterial infections and colonization by participating in innate immune system. Scanlon et  al. used the concept of protein engineering to design the human

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Glu35

O O

RO

O

NH O

OH O

OH

H2O

NH

HO O

O

O

HO

OH

O

O O

RO

NH

HO HO

OH

O

NH O

OH

n

OAsp53

O

O

OAsp53

Fig. 1.1  Lysozyme (hLYS) catalyzes hydrolysis of peptidoglycan. A line drawing representing the two repeating carbohydrate units of the bacterial cell wall: (1,4)-linked N-acetyl muramic acid and N-acetyl glucosamine. The catalytic residues of hLYS are shown in gray. The “R” group of N-acetyl muramic acid represents a C2-ether-linked lactic acid moiety that is in turn coupled to adjacent polysaccharide chains via short, cross-linking polypeptides. The resulting macromolecular net surrounds individual bacteria and forms the protective sacculus that opposes osmotic stress. Sacculus integrity and cell viability are compromised by hLYS-catalyzed hydrolysis of the polysaccharide chains. Reprinted with permission from Scanlon et al. (2010). Enhanced anti-microbial activity of engineered human lysozyme. ACS Chem Biol 5:809–818 (Scanlon et  al. 2010). Copyright © 2010 American Chemical Society

lysozyme and showed their mechanisms for enhanced anti-microbial activity (Fig. 1.1) (Scanlon et al. 2010). Additionally, the mechanism of action can be enzymatic (muramidase-dependent) or non-enzymatic (membrane perturbing) (Callewaert and Michiels 2010; Callewaert et al. 2012; During et al. 1999; Scanlon et al. 2010). Lysozyme increases the phagocytic activity of some leukocytes (polynuclear) and macrophages non-specifically which supports the immunoregulatory activity of the same (Ye et al. 2008). According to Bruzzesi et al., the monomer of lysozyme undergoes dimeric association which is a pH-dependent reversible process (Bruzzesi et al. 1965).

1.1.3 Application in Different Fields Lysozyme has various biological applications like anti-microbial, anti-proliferative, and amyloid-forming ability.

1.1.3.1 Anti-Microbial Activity Lysozyme exhibits enhanced anti-microbial activity. Generally, in human airway fluids lysozyme is the most effective cationic anti-pseudomonal agent (Cole et al. 2002). However, the wild-type human lysozyme is not able to perform well in specific lung environment during chronic infections. Recombinant human lysozyme can be used as a therapeutic protein if properly delivered by inhalation techniques (Shire 1996). Alleviating the functional limitations of the wild-type human lysozyme may help in the development of new anti-microbial therapies. Because of the cationic (positive) nature of the human lysozyme, it is thought that it can be used to

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attract the negatively charged bacterial cell wall. In some cases, due to the dense cationic charge, hLYS (human lysozyme) can bind with alginate and turns it into its inactivated form (Scanlon et al. 2010). In order to decrease the immunogenic effect of the enzyme, Gill et al. used human scaffold protein as the starting template. The authors demonstrated that charge-engineered human lysozymes could be created with the help of bio-informatics and structural analysis techniques (Gill et al. 2011). The authors reported that the re-shaped electrostatic potential of bio-therapeutic candidates delivered enhanced inhibitory effect against gram-positive (M. luteus) and gram-negative (P. aeruginosa) bacteria. Additionally, the group demonstrated that even after modifying the amino acid residues in the variant form, the stability and global structure were similar to the wild-type form. Finally, the authors shed lights on the future applicability of the modified human lysozyme for the treatment of the CF (cystic fibrosis) as well as COPD (chronic obstructive pulmonary diseases). Sometimes, in case of acute and chronic diseases, huge amount of anionic biopolymer accumulated which concomitantly decreases lysozyme activity. In order to overcome the pitfalls, human lysozyme was modified with the help of the protein engineering useful for airway infections. Scanlon et al. functionally interrogated the human lysozyme (charge-engineered) using a novel high-throughput screen method (Scanlon et  al. 2010). The group used a mouse model having acute pulmonary infections (Pseudomonas aeruginosa bacterial strain) which showed a large gathering of biopolymers (anionic) that passively deteriorate the lysozyme activity. The authors illustrated the idea that in the presence of biopolymer (disease-associated), reduction in the net cationic character improved the anti-microbial activity. Finally, the authors concluded that the hLYS acted as an adaptable scaffold on which variant antibiotics (biocatalytic) can be engineered. Hughey et al. demonstrated that lysozyme can act as a food preservative by preventing the spoilage of food from bacterial contamination (Hughey and Johnson 1987). The authors mentioned that four strains of L. monocytogenes (infected in human through vegetables, milk products like whole milk or soft cheese) as well as few strains of C. botulinum could be lysed by the lysozyme activity. The group demonstrated that lysozyme in association with EDTA exhibited enhanced activity in a consistent manner. The authors explained that by associating lysozyme with the EDTA increased the activity by removing cell wall components and exposing the peptidoglycan layer toward lysozyme’s active site. Finally, the authors mentioned that the rate of bacterial degradation was high enough in low temperature compared to the higher temperature.

1.1.3.2 Anti-Proliferative Activity of Lysozyme Apart from the anti-microbial activity, the lysozyme can also act as an anti-­ proliferative agent. It is deeply associated with monocyte–macrophage system for non-specific defense mechanism (Osserman 1976). It has been reported that it is generally expressed in gastric Paneth cells as well as having an efficient effect on malignant tumors. Guo et  al. demonstrated the anti-proliferative activity toward gastric cancer cells (MGC803, MKN28, and MKN45) as well as normal fibroblast (human lung) of recombinant human lysozyme (rHlys) (Guo et  al. 2007). The authors showed that rHlys displayed inhibiting activity of gastric cells at higher

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concentrations, whereas at concentration lower than that it triggered the proliferation surprisingly. The authors claimed that 100 μg/l was the optimum growth inhibiting concentrations. Finally, the group provided a ray of hope for the future application of recombinant human lysozyme as an anti-proliferative agent in future. Similarly, Ye et al. reported the anti-proliferative activity of marine-derived lysozyme both in vitro and in vivo conditions (Ye et al. 2008). The authors reported that the marine-derived lysozyme hindered the proliferation of the endothelial cells as well as retarded neovasculature in chicken embryos in a dose-dependent manner. Furthermore, the group mentioned that the lysozyme significantly inhibited the growth of tumor in tumor-bearing mice (hepatoma 22 or sarcoma 180). The marine-­ derived lysozyme exhibited dose-dependent reduction of the branch points when treated on the hen egg, whereas the hen-derived lysozyme did not show any decrease in branches (Fig. 1.2). The PBS control group also exerted the similar effects like hen-derived lysozyme. Finally, the authors claimed that due to several advantages (abundance, cold-adaption property, optimum temperature stability, easier extraction property, etc.) of the marine-derived lysozyme, it could be useful for anti-­ proliferative activity. Similarly, Mahanta et  al. designed self-assembled nanostructured lysozyme (snLYZ) using simple de-solvation technique (Mahanta et al. 2015). The self-assembled nanostructure was further characterized using the different physico-chemical techniques. The as-synthesized snLYZ nanostructured lysozyme displayed excellent structural and functional stability in wide ranges of pH.  The authors mentioned that the snLYZ exhibited excellent anti-proliferative activity toward human breast cancer cell line MCF-7 compared to the native lysozyme through ROS generation pathway. Additionally, the authors revealed that the hemocompatible snLYZ displayed more cell-killing ability when tagged with folic acid. Finally, the authors shed lights on the future application of the nanostructure in tissue engineering and regenerative medicine.

1.1.3.3 Amyloid-Forming Ability Whenever there are mutations in the genes coding for lysozyme, it gives rise to lysozyme amyloidosis. In order to study the effect, Helmfros et al. expressed the disease-associated variant F57I with normal wild-type variant (human) lysozyme in the central nervous system of Drosophila melanogaster model in association with

Fig. 1.2  Effect of marine lysozyme on CAM. Fertilized eggs were incubated continuously for 6 days, and then a window was opened to expose the CAM, and lysozyme at different concentrations was added on sterilized filter paper discs on day 7. The eggs were incubated for another 72 h, and then the treated CAMs were harvested and photographed. (a) 0 nM/egg (PBS negative control), (b) 1.2  nM/egg (marine lysozyme), (c) 1.2  nM/egg (hen egg lysozyme), (d) 100  nM/egg (suramin). (e) Macroscopic assessment of vascular density conducted by counting the number of branch points within a 100-mm2 area surrounding filter paper in each photograph. The number of branch points was markedly decreased with marine lysozyme in a dose-dependent manner compared to PBS control; there are no obvious differences between hen egg lysozyme-treated groups and PBS control (n  =  8; mean  ±  SEM); double asterisk p