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Bioanalytical Techniques

Principles and Applications

Edited by Inamuddin, Tariq Altalhi, Abeer Alosaimi and Jorddy Neves Cruz
Copyright: 2025   |   Status: Published
ISBN: 9781394314102  |  Hardcover  |  
710 pages
Price: $225 USD
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One Line Description
The book provides a comprehensive guide that covers the fundamental principles and methodologies of essential bioanalytical techniques.

Audience
Biochemists, biologists, chemists, and medical and pharmaceutical professionals interested in biomolecules, enzymology, and biochemical pathways.

Description
Bioanalytical Techniques: Principles and Applications is a comprehensive and authoritative book that explores the principles, methodologies, and applications of bioanalytical techniques in the field of life sciences. The book covers a wide range of analytical techniques used for the characterization, quantification, and analysis of biological samples, including proteins, nucleic acids, metabolites, and biomarkers. Using a multidisciplinary approach by integrating concepts from biochemistry, molecular biology, analytical chemistry, and biotechnology, this book provides a solid foundation in the fundamental principles underlying various bioanalytical techniques, such as spectroscopy, chromatography, electrophoresis, immunoassays, mass spectrometry, and biosensors. Each technique is explained in detail, including its working principles, instrumentation, data analysis, and practical considerations. The book incorporates case studies, examples, and practical tips to illustrate how these techniques are used to solve biological problems and address research questions. It also discusses emerging trends and technologies in bioanalytical techniques, such as microfluidics, nanotechnology, and omics approaches.
Readers will find the book:
• Offers comprehensive coverage of bioanalytical techniques, encompassing a wide range of methodologies, instruments, and applications through real-world case studies;
• Adopts a multidisciplinary approach, integrating concepts from biochemistry, molecular biology, analytical chemistry, and biotechnology;
• Explores emerging trends and technologies in bioanalytical techniques, such as microfluidics, nanotechnology, omics approaches, and bioinformatics;
• Includes practical guidance, troubleshooting tips, and common challenges in bioanalysis, equipping readers with valuable insights and strategies for successful experimentation and data interpretation;
• Features contributions from renowned experts and leaders in the field, ensuring the content is authoritative, up-to-date, and reflects the latest advancements in bioanalytical techniques.

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Author / Editor Details
Inamuddin, PhD, is an assistant professor at the Department of Applied Chemistry, Zakir Husain College of Engineering and Technology, Faculty of Engineering and Technology, Aligarh Muslim University, Aligarh, India. He has extensive research experience in multidisciplinary fields of analytical chemistry, materials chemistry, electrochemistry, renewable energy, and environmental science. He has worked on different research projects funded by various government agencies and universities and is the recipient of awards, including the Department of Science and Technology, India, Fast-Track Young Scientist Award and Young Researcher of the Year Award 2020 from Aligarh Muslim University. He has published about 210 research articles in various international scientific journals, many book chapters, and dozens of edited books, many with Wiley-Scrivener.

Tariq Altalhi, PhD, is an associate professor in the Department of Chemistry at Taif University, Saudi Arabia. He received his doctorate degree from the University of Adelaide, Australia in 2014 with Dean’s Commendation for Doctoral Thesis Excellence. He has worked as head of the Chemistry Department at Taif University and Vice Dean of Science College. In 2015, one of his works was nominated for Green Tech awards from Germany, Europe’s largest environmental and business prize. He has also co-edited a number of scientific books.

Abeer Alosaimi, PhD, is an assistant professor in the Department of Chemistry at Taif University, Saudi Arabia with over 22 years of academic experience. He has over 50 publications, including one book and articles in international journals and conferences. His research interests include polymer science, nanocomposites, and organic chemistry.

Jorddy Neves Cruz is a researcher at the Federal University of Pará and the Emilio Goeldi Museum, Brazil. He has experience in multidisciplinary research in the areas of medicinal chemistry, drug design, extraction of bioactive compounds, extraction of essential oils, food chemistry and biological testing. He has published several research articles in scientific journals and is an associate editor of the Journal of Medicine.

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Table of Contents
Preface
1. Point-of-Care Diagnostics for Rapid Disease Detection
Nabil H. Bhuiyan and M. Khalid Hossain
1.1 Introduction
1.2 Fundamentals of Point-of-Care Diagnostics
1.3 Technologies Driving Point-of-Care Diagnostics
1.3.1 Lateral Flow Assay (LFA)
1.3.2 Enzyme-Linked Immunosorbent Assay (ELISA)
1.3.3 Nucleic Acid Amplification Techniques
1.3.4 Electrochemical Biosensors
1.3.5 Lab-on-a-Chip Devices
1.3.6 Wearable Healthcare Device-Based POC Diagnostics
1.3.7 Smartphone-Based POC Diagnostics
1.3.8 Spectroscopic Techniques for POC
1.4 Challenges and Advances in Point-of-Care Diagnostics
1.5 Future Directions and Trends
1.6 Ethical Considerations
1.7 Conclusion
References
2. Principles of Molecular Biology for Bioanalysis
Syed Ali Raza Naqvi, Syeda Marab Saleem, Tania Jabbar, Atta Ul Haq, Muhammad Asif , Sadaf Ul Hassan, Muhammad Rehan Hasan Shah Gilani, Naseem Abbas and Ali Abbas
2.1 Introduction
2.2 Central Dogma of Molecular Biology
2.2.1 DNA Structure and Function
2.2.1.1 DNA Double Helix
2.2.1.2 DNA Replication
2.2.2 RNA Structure and Function
2.2.2.1 Transcription
2.2.3 Protein Structure and Function
2.3 Nucleic Acid Extraction and Purification
2.4 Amplification Techniques
2.4.1 Polymerase Chain Reaction (PCR)
2.4.2 Reverse Polymerase Chain Reaction (R-PCR)
2.4.3 Quantitative Polymerase Chain Reaction (q-PCR)
2.4.4 Isothermal Amplification Techniques
2.5 Nucleic Acid Sequencing
2.5.1 Sanger Sequencing
2.5.2 Next Generation Sequencing
2.5.2.1 Whole-Genome and Whole-Exome Sequencing
2.5.2.2 Targeted Sequencing
2.5.2.3 Pyrosequencing
2.5.3 Application in Bioanalysis
2.5.3.1 DNA Sequencing Techniques
2.5.3.2 PCR
2.5.3.3 Capillary Electrophoresis (CE)
2.6 Molecular Probes and Labels
2.7 Nucleic Acid Based Assay
2.7.1 Blotting
2.7.1.1 Southern Blotting
2.7.1.2 Northern Blotting
2.7.1.3 Western Blotting
2.7.2 Nucleic Acid Probes in Bioanalysis
2.7.3 Enzyme Linked Immunosorbent Assay (ELISA)
2.7.4 In Situ Hybridization Techniques
2.7.4.1 Fluorescent In Situ Hybridization
2.7.4.2 PCR In Situ
2.7.4.3 CISH
2.8 Conclusion and Future Prospective
References
3. UV–Visible Spectroscopy for Quantitative Analysis of Biomolecules
Syeda Marab Saleem, Syed Ali Raza Naqvi, Muhammad Ramzan Saeed Ashraf Janjua, Tauqir A. Sherazi, Muhammad Saeed, Sadaf Ul Hassan, Muhammad Imran,
Muhammad Asif, Mamoon Ur Rasheed and Tania Jabbar
3.1 Introduction
3.2 Principles of UV–Visible Spectroscopy
3.3 Components of UV–Visible Spectrophotometer
3.3.1 Light Source
3.3.2 Monochromator
3.3.2.1 Components of Monochromator
3.3.3 Sample Device
3.3.4 Detector
3.3.4.1 Photovoltaic Cells
3.3.4.2 Phototubes or Photoemissive Tubes
3.3.4.3 Photomultiplier Tubes
3.3.4.4 Photodiode Detector Array
3.3.5 Recorder
3.4 UV–Vis Spectrophotometer Types
3.4.1 Single-Beam Spectrophotometer
3.4.2 Double-Beam Spectrophotometer
3.5 Applications of UV–Visible Spectroscopy in Analysis of Biomolecules
3.5.1 Proteins
3.5.1.1 Direct Absorbance Measurements
3.5.1.2 Derivatization
3.5.1.3 Biuret Method
3.5.1.4 Lowry Method
3.5.1.5 Bradford Method
3.5.1.6 BCA Method
3.5.1.7 Advantages and Disadvantages of Using UV–Visible Spectroscopy for Protein Quantification
3.5.2 Lipids
3.5.2.1 Colorimetric Methods for Lipid Quantification
3.5.2.2 Analyzing Noncovalent Complexes with Aromatic Molecules
3.5.2.3 Identification and Extraction Kinetics of Lipids
3.5.2.4 Oxidation of Lipids
3.5.2.5 Advantages and Disadvantages of Using UV–Visible Spectroscopy for Lipid
Quantification
3.5.3 Nucleic Acid
3.5.3.1 DNA Quantification
3.5.3.2 Study of DNA Stability
3.5.4 Quantification of Carbohydrates Using UV–Visible Spectroscopy
3.5.4.1 Phenol Sulfuric Acid Method
3.5.5 Biomolecular Interaction Analysis
3.6 Other Applications of UV–Visible Spectroscopy
3.6.1 Determination of Molecular Weight
3.6.2 Detection of Impurities
3.6.3 Qualitative Pharmaceutical Evaluation
3.6.4 Functional Group Evaluation
3.7 Future Perspectives and Advances
3.7.1 Nanomaterials and Plasmonics
3.7.2 Single-Molecule Spectroscopy
3.7.3 Multidimensional Spectroscopy
3.7.4 Imaging and Mapping Techniques
3.7.5 Integration with Other Techniques
3.8 Conclusion
References
4. Emerging Trends and Future Perspectives in Bioanalysis
Jayapal Reddy Gangadi, Kalpana Swain and Satyanarayan Pattnaik
4.1 Introduction
4.2 Single-Cell Analysis
4.2.1 Applications in Developmental Biology and Disease Research
4.2.2 Challenges and Future Horizons
4.3 Artificial Intelligence in Bioanalysis
4.3.1 Data Processing and Pattern Recognition
4.3.2 Predictive Modeling
4.3.3 Optimizing Experimental Design
4.3.4 Challenges and Ethical Considerations
4.4 Microfluidics and Lab-on-a-Chip Technologies
4.4.1 The Essence of Microfluidics
4.4.2 Lab-on-a-Chip
4.4.3 Challenges and Opportunities
4.5 Biosensors and Wearable Devices
4.5.1 Wearable Devices
4.5.2 Challenges and Way Ahead
4.6 Environmental Bioanalysis
4.6.1 Environmental DNA (eDNA) Analysis
4.6.2 Biomarker Detection in Organisms
4.6.3 Applications of Environmental Bioanalysis
4.6.4 Challenges and Way Ahead
4.7 Future Perspectives of Bioanalysis
4.7.1 Integration of Emerging Technologies
4.7.2 Single-Cell Omics Revolution
4.7.3 Spatial Omics and 3D Imaging
4.7.4 Advanced Gene Editing Technologies
4.7.5 Point-of-Care Diagnostics and Decentralized Bioanalysis
4.7.6 Sustainable and Environmental Bioanalysis
4.7.7 Ethical Considerations and Responsible Innovation
4.8 Conclusion
References
5. Introduction to Biosensors for Point‑of-Care Testing: IoT-Based Vitamin D3 Biosensor
Asif Hussain Shaik and Chinna Babu Jyothi
5.1 Introduction
5.2 Literature Review
5.2.1 The Problem Statement
5.2.2 Proposed System
5.2.3 Vitamin D3: Academic, Scientific, and Innovative Significance
5.2.4 Benefits to Oman
5.3 Conclusion and Recommendations
References
6. Fluorescence Spectroscopy for Protein–Protein Interactions
Masoud Shayegan and Hossein Ahmadzadeh
6.1 Introduction
6.1.1 Basic Concepts of Fluorescence
6.1.2 Fluorophores and their Properties
6.1.2.1 Spectral Characteristics
6.1.2.2 Quantum Yield (QF)
6.1.2.3 Lifetime
6.1.2.4 Photostability
6.1.2.5 Biocompatibility
6.1.3 Fluorescence Emission Spectra and Stokes Shift
6.1.4 Fluorescence Lifetime and Quenching
6.1.5 Anisotropy and Polarization Measurements
6.2 Experimental Techniques in Protein–Protein Interaction Analysis
6.2.1 Fluorescence Intensity Measurements
6.2.2 Fluorescence Correlation Spectroscopy (FCS)
6.2.3 Time-Resolved Fluorescence Spectroscopy
6.2.4 Fluorescence Resonance Energy Transfer (FRET)
6.2.5 Fluorescence Lifetime Imaging Microscopy (FLIM)
6.3 Practical Examples of Protein–Protein Interaction Studies
6.3.1 Case Study 1
6.3.2 Case Study 2
6.4 Conclusion
References
7. Flow Cytometry for Cell Analysis and Sorting
Maryam Davardoostmanesh and Hossein Ahmadzadeh
7.1 Introduction
7.2 Components of a Flow Cytometer
7.2.1 Fluidics
7.2.2 Optics and Electronic
7.3 Basic Principles of Fluorescence
7.4 Scattering
7.5 Applications
7.5.1 Sorting Cells by Flow Cytometry
7.5.2 General Considerations in Cell Sorting
7.6 Chemical Cytometry
7.7 Future Perspectives
References
8. Application in Drug Discovery and Development for Lead Identification
Sareena Ehsan, Rida Mumtaz, Abdul Rehman, Maryam, Habibullah Nadeem, Ammara Riaz, Jallat Khan, Ebrahim Alinia-Ahandani and Zeliha Selamoglu
8.1 Introduction
8.2 Screening of Compound
8.2.1 Mass Spectrometry-Based Method
8.3 Identification and Characterization of Potential Lead Compounds
8.3.1 Identification and Characterization
8.3.2 Aiding in Drug Candidate Analysis
8.4 Separation of Lead Compounds from Complex Samples
8.5 NMR as a Precision Tool in Lead Identification
8.6 Conclusion
References
9. Immunoblotting Techniques for Protein Identification and Quantification and Its Application
Megha Sikder, Somen Debnath and Biswanath Bhunia
9.1 Introduction
9.2 The History Behind Immunoblotting Techniques
9.3 Steps Involved in Immunoblotting Techniques
9.3.1 Sample Preparation
9.3.2 Electrophoresis
9.3.3 Membrane Transfer
9.3.4 Blocking
9.3.5 Probe Detection
9.4 Applications of Immunoblotting Techniques
9.4.1 Diagnosis of Different Diseases
9.4.2 Getting a New Direction in Cancer Research
9.4.3 In Attempt to Find a Vaccine for Pneumococcal Disease
9.4.4 Identifying AIDs and Associated Diseases
9.4.5 Finding Cure for Hepatitis C
9.5 Latest Trends in Immunoblotting Techniques
9.6 Conclusion
References
10. Gel Electrophoresis for DNA Fragment Analysis
Aneela Nawaz, Shahzar Khan, Momina Aamir, Sidra Zaheer, Sabeena Zafar, Nauman Ahmed Khalid and Samiullah Khan
10.1 Introduction
10.1.1 History of Electrophoresis
10.1.2 Principle
10.1.3 Procedure of DNA Gel Electrophoresis
10.2 Types of Gel Electrophoresis
10.2.1 Agarose Gel Electrophoresis
10.2.2 Polyacrylamide Gel Electrophoresis
10.2.3 Native Gels
10.2.4 Pulsed-Field Gel Electrophoresis
10.2.5 Denaturing Gradient Gel Electrophoresis (DGGE)
10.2.6 Two-Dimensional Gel Electrophoresis
10.2.7 Capillary Electrophoresis
10.2.8 Affinity Electrophoresis
10.3 Types of Buffer and Its Limitations
10.4 Pros and Cons of Stains Used
10.5 Recent Advancements in Gel Electrophoresis
10.6 Limitations of Gel Electrophoresis
10.7 Applications
10.8 Conclusion
References
11. Omics Approaches in Bioanalysis for Systems Biology Studies
Rana Hooshang, Hoda Nouri and Hamid Moghimi
Abbreviation
11.1 Background: History
11.2 Genomics
11.2.1 Structural Genomics
11.2.1.1 Next Generation Sequencing
11.2.1.2 Sequence Assembly, Gene Annotation, and Ontology
11.2.2 Comparative Genomics
11.2.3 Metagenomics
11.2.3.1 Metagenomics and Systems Biology
11.2.3.2 Tools and Pipelines
11.2.4 Functional Genomics
11.3 Transcriptomics
11.3.1 Serial/Cap Analysis of Gene Expression (SAGE)
11.3.2 RNA-Seq
11.4 Proteomics
11.4.1 Mass Spectrometry (MS)
11.4.2 Protein Microarray
11.4.3 Yeast Two-Hybrid Method
11.5 Metabolomics
11.5.1 From Metabolites to Metabolomics
11.5.2 Computational Methods for Metabolome Data Analysis
11.6 Fluxomics
11.7 Multi-Omics: Omics Dataset Integration
11.8 Systems Biology
11.8.1 Genome-Scale Metabolic Network Models
11.8.1.1 Metabolic Model Draft Reconstruction
11.8.1.2 Model Refinement
11.8.1.3 Mathematical Representation of the Metabolic Network
11.8.2 Regulatory Network Models
11.8.2.1 Regulatory Model Reconstruction
11.8.3 Signaling Network Models
11.8.3.1 Signaling Model Reconstruction
11.8.3.2 Case Studies in Signaling Network
11.8.4 Interactome
11.9 Conclusion
References
12. Introduction to Mass Spectrometry for Metabolite Profiling
Jackie E. Wood and Brendon D. Gill
12.1 Introduction
12.2 Analysis of Samples
12.2.1 Standards and Quality Control
12.2.2 Sample Preparation
12.2.3 Sample Introduction
12.3 Mass Spectrometry
12.3.1 Ionization
12.3.2 Mass Analyzers
12.3.3 Multiple Mass Analyzers
12.3.4 Chromatographic Separation
12.4 Processing the Data
12.4.1 Workflows
12.4.2 Annotating Libraries and Databases
12.4.3 Noise Reduction
12.4.4 Normalization Strategies
12.4.5 Missing Values
12.4.6 Adducts
12.4.7 Outliers
12.4.8 Data Processing Packages
12.5 Data Analysis
12.5.1 Graphs and Univariate Analysis
12.5.2 Multivariate Statistical Analysis
12.5.3 Machine Learning Techniques
12.5.4 Pathway Analysis
12.6 Applications
12.6.1 Plants
12.6.2 Humans
12.6.3 Other Animals
12.6.4 Microbes
12.6.5 Foods
References
13. Infections, Symptoms, and Clinical Diagnostic Techniques for Dengue: A Case Study of a Neglected Tropical Disease
Shreeganesh Subraya Hegde and Badekai Ramachandra Bhat
13.1 Introduction
13.2 Dengue: A Neglected Tropical Disease
13.3 Dengue Biosensor
13.4 Conclusions
References
14. Microfluidic-Based Bioassays for High-Throughput Analysis
Muthui Martin Mwaurah, J. Mathiyarasu and A.M. Vinu Mohan
14.1 Introduction
14.2 What is High-Throughput Analysis?
14.3 Microfluidic Platforms for High-Throughput Analysis
14.3.1 Materials for Microfluidic Devices
14.3.2 Fabrication of Microfluidic Devices
14.3.2.1 Fabrication of Paper-Based Microfluidic Devices
14.3.2.2 Fabrication of Advanced Microfluidic Devices
14.4 Detection Methods
14.5 Bioassays
14.5.1 Cell-Based Bioassays
14.5.2 Whole-Organism Bioassays
14.5.3 Immunobioassays
14.5.4 Enzyme Bioassays
14.5.5 Aptamer-Based Bioassays
14.6 Conclusion and Future Perspectives
Acknowledgments
References
15. Circular Dichroism Spectroscopy for Secondary Structure Analysis of Proteins
Masooma Siddiqui, Maroof Ali, Mehak Sagheer and Mohd Imran Ahamed
15.1 Introduction
15.2 Principles of Circular Dichroism Spectroscopy
15.2.1 Basics of CD Spectroscopy
15.2.2 Secondary Structure Contributions
15.2.2.1 What are the Limitations of Using CD Spectroscopy to Estimate Protein
Secondary Structure?
15.3 Instrumentation
15.3.1 CD Spectrophotometer
15.3.2 Sample Preparation
15.3.2.1 Choice of Buffer
15.3.2.2 pH Adjustment
15.3.2.3 Sample Purity and Concentration
15.3.2.4 Sample Handling
15.3.2.5 Cuvette Selection
15.3.2.6 Reference Cell
15.3.2.7 Temperature Control
15.4 Data Analysis
15.4.1 Estimation of Secondary Structure
15.4.1.1 Deconvolution Methods
15.4.1.2 Reference Databases
15.4.1.3 Basis Set Selection
15.4.1.4 Regularization
15.4.1.5 Estimation Output
15.4.1.6 Validation and Interpretation
15.4.1.7 Limitations and Considerations
15.4.2 Thermal Denaturation Studies
15.4.2.1 Data Acquisition
15.4.2.2 Baseline Correction
15.4.2.3 Data Normalization
15.4.2.4 Calculation of Fraction Unfolded
15.4.2.5 Fitting to a Two-State Model
15.4.2.6 Interpretation of Tm and Thermodynamic Parameters
15.4.2.7 Considerations and Limitations
15.5 Applications
15.5.1 Protein Folding Studies
15.5.1.1 Monitoring Secondary Structure Changes
15.5.1.2 Characterizing Folding Pathways
15.5.1.3 Kinetic Studies
15.5.1.4 Stability Assessments
15.5.1.5 Unfolding Studies
15.5.1.6 Disease-Related Folding Studies
15.5.1.7 Biotechnology and Protein Engineering
15.5.2 Drug Discovery and Development
15.5.2.1 Protein–Ligand Interactions
15.5.2.2 Ligand Screening and Characterization
15.5.2.3 Protein Stability Assessment
15.5.2.4 Mechanistic Studies
15.5.2.5 Enantiomer Differentiation
15.5.2.6 Validation of Protein Targets
15.5.2.7 Membrane Protein Studies
15.5.3 Structural Biology
15.5.3.1 Secondary Structure Analysis
15.5.3.2 Membrane Protein Studies
15.5.3.3 Protein Conformational Changes
15.5.3.4 Protein–Ligand Interactions
15.5.3.5 Mechanistic Studies
15.5.3.6 Protein–Protein Interactions
15.5.3.7 Structural Validation
15.5.3.8 Disease-Related Studies
15.6 Recent Advances: Exploring New Frontiers
15.6.1 Membrane Protein Analysis
15.6.1.1 Native Lipid Environment Studies
15.6.1.2 High-Throughput Screening
15.6.1.3 Temperature-Jump CD
15.6.1.4 Advanced Data Analysis
15.6.1.5 Coupling with Other Techniques
15.6.1.6 In-Cell and In Vivo Studies
15.6.1.7 Integration of Computational Modeling
15.6.1.8 Functional Analysis
15.6.2 Time-Resolved CD Spectroscopy
15.6.2.1 Ultrafast Time Resolution
15.6.2.2 Multiplexed Detection
15.6.2.3 Expanded Wavelength Ranges
15.6.2.4 Biomolecular Systems
15.6.2.5 Integration with Other Techniques
15.6.2.6 Structural Insights into Disease-Related Processes
15.6.2.7 Functional Dynamics
15.6.2.8 In Vivo and Cellular Studies
15.6.3 Chiroptical Sensors for In Vivo Studies
15.6.3.1 Chiral Sensing in Complex Biological Environments
15.6.3.2 Imaging and Visualization
15.6.3.3 Biomarker Detection
15.6.3.4 Pharmacokinetics and Drug Development
15.6.3.5 Nanotechnology Integration
15.6.3.6 Targeted Therapies
15.6.3.7 Microfluidics and Miniaturization
15.7 Conclusion
15.7.1 Unravelling the Complexity of Biomolecules
15.7.2 Understanding Protein Folding and Stability
15.7.3 Drug Discovery and Structural Biology
15.7.4 Membrane Protein Analysis
15.7.5 Chiroptical Sensors for In Vivo Studies
15.7.6 Multidisciplinary Collaborations
15.7.7 Future Horizons and Challenges
15.7.8 Education and Accessibility
15.7.9 Ethical and Responsible Research
References
16. Optical Biosensors for Detection of Analytes in Biological Samples
Uzma, Masooma Siddiqui and Mehtab Parveen
16.1 Introduction
16.1.1 Significance of Biosensors in Biomedical Research
16.1.2 Optical Biosensors: A Principles Shift in Bioanalysis
16.1.3 The Growing Demand for Advanced Detection Technologies
16.1.4 Aim of This Chapter
16.1.5 Structure of the Chapter
16.2 Principles of Optical Biosensors
16.2.1 Surface Plasmon Resonance (SPR): Illuminating Molecular Interactions
16.2.2 Fluorescence: Illuminating the Molecular Signature
16.2.3 Evanescent Wave Sensing: Probing Beyond the Surface
16.2.4 Total Internal Reflection: Guiding Light for Precision
16.2.5 Interaction of Light with Biological Molecules: Unveiling Molecular Fingerprints
16.3 State-of-the-Art Technologies in Optical Biosensors
16.3.1 Plasmonic Nanomaterials: Enhancing Sensitivity Through Precision
16.3.1.1 Principles of Plasmonic Nanomaterials: Resonating with Light
16.3.1.2 Tuning Sensitivity Through Nanomaterial Design: Size, Shape, and Composition
16.3.1.3 Amplifying Signals for Enhanced Sensitivity: Surface-Enhanced Raman
Scattering (SERS) and Beyond
16.3.1.4 Biocompatibility and Stability Challenges: Navigating the Nanoscale
16.3.1.5 Applications in Biosensing: From Biomolecular Interactions to Disease
Diagnostics
16.3.2 Photonic Crystal Biosensors: Unraveling Label-Free Detection
16.3.2.1 Photonic Crystal Structures: Architectural Foundations
16.3.2.2 Label-Free Detection Mechanism: Probing Biomolecular Binding Events
16.3.2.3 Sensitivity Enhancement: Tailoring Resonances for Precision
16.3.2.4 Real-Time Monitoring of Biomolecular Interactions: Dynamic Insights
16.3.2.5 Applications in Label-Free Biosensing: From Biomarker Detection to Drug
Screening
16.3.3 Whispering Gallery Mode Resonators: Harnessing High-Q Optical Microresonators
16.3.3.1 Principles of Whispering Gallery Modes: Circles of Optical Resonance
16.3.3.2 Fabrication Techniques: Crafting Precision in Microresonators
16.3.3.3 Sensing Mechanism: Probing Minute Changes in Refractive Index
16.3.3.4 Applications in Biosensing: From Single-Molecule Detection to Biomolecular Interaction Studies
16.3.3.5 Challenges and Future Directions: Navigating Towards Practical Implementation
16.3.4 Quantum Dots and Up-Conversion Nanoparticles: Illuminating Fluorescence-Based Biosensing
16.3.4.1 Quantum Dots: Semiconducting Brilliance
16.3.4.2 Upconversion Nanoparticles: Shining Beyond the Limits of Excitation
16.3.4.3 Fluorescence Resonance Energy Transfer (FRET): Amplifying Signals Through Nano Proximity
16.3.4.4 Multiplexing Capabilities: Painting a Fluorescent Palette
16.3.4.5 Applications in Biosensing: From Disease Markers to Intracellular Probes
16.4 Applications in Biomedical Research
16.4.1 Medical Diagnostics: Precision in Disease Detection
16.4.1.1 Mechanisms of Detection: Unravelling Molecular Signatures
16.4.1.2 Examples of Cardiac Biomarker Detection: Paving the Way for Precision
Cardiovascular Diagnostic
16.4.1.3 Infectious Diseases: Rapid and Accurate Pathogen Detection
16.4.1.4 Neurodegenerative Disorders: Illuminating Molecular Markers
16.4.2 Environmental Monitoring: Probing the Impact of Biological and Chemical Agents
16.4.2.1 Detection of Waterborne Pathogens: Safeguarding Water Quality
16.4.2.2 Air Quality Monitoring: Assessing Contaminant Levels
16.4.2.3 Soil Contamination Detection: Monitoring Environmental Health
16.4.2.4 Early Warning Systems for Environmental Threats: Beyond Detection
16.4.2.5 Biodiversity Monitoring: Studying Ecosystem Health
16.4.3 Drug Development: Accelerating Discovery and Analysis
16.4.3.1 Screening of Drug–Receptor Interactions: Expediting Target Identification
16.4.3.2 Evaluation of Cellular Responses: Probing Mechanisms of Action
16.4.3.3 Assessment of Drug Efficacy and Toxicity: Balancing Benefits and Risks
16.4.3.4 Personalized Medicine: Tailoring Treatments to Individual Responses
16.4.3.5 Integration of Optical Biosensors with High-Throughput Technologies: Scaling Efficiency
16.5 Challenges and Future Perspectives
16.5.1 Stability and Reproducibility: Ensuring Robust Performance
16.5.2 Integration into Point-of-Care Devices: Bridging the Gap to Practical Application
16.5.3 Multianalyte Detection: Meeting the Demands of Complexity
16.5.4 Emerging Analytes and Sample Matrices: Expanding the Scope
16.5.5 Artificial Intelligence Integration: Enhancing Analytical Capabilities
16.6 Conclusion
References
17. Tandem Mass Spectrometry for Peptide Sequencing
Satyendra Mishra and Neha V. Rathod
17.1 Introduction
17.1.1 Importance of Peptide Sequencing and the Role of Tandem Mass Spectrometry
17.2 Instrumentation Tandem Mass Spectrometry
17.2.1 Ion Source
17.2.2 Mass Analyzer
17.2.3 Collision Cell
17.2.4 Detector
17.3 Fundamental Technique for Tandem Mass Spectrometry
17.3.1 Tandem-in-Space MS
17.3.2 Tandem-in-Time MS
17.4 Peptide Fragmentation Process
17.5 Mass Determination
17.5.1 Interpretation and Analysis of Mass Spectra of Peptide Sequencing
17.5.2 Database Search
17.5.3 De Novo Sequencing
17.6 Conclusion
References
18. Unraveling Complexity: Cutting-Edge Ion Chromatography Methods for the Analysis of Inorganic Ions in Biological Samples
Muhammad Hafiznur Yunus, Nor Ain Shahera Khairi, Azren Aida Asmawi, Fatin Nabilah Mohd Faudzi, Ahmad Farabi Mohamad Saman, Nor Azah Yusof and Siti Fatimah Nur Abdul Aziz
18.1 Introduction
18.2 The Dichotomy of Challenges and Prospects in Ion Chromatography Implementation
18.3 Delving into the Core Principles of Ion Chromatography
18.3.1 Basic Principles and Diverse Modes of Separation in Ion Chromatography
18.3.2 Ion-Exchange Chromatography
18.3.3 Ion-Exclusion Chromatography
18.3.4 Ion-Pair Chromatography
18.4 Sample Preparation in Ion Chromatography: Techniques and Best Practices
18.4.1 Sample Preparation for Solid Samples
18.4.1.1 Dry Ashing
18.4.1.2 Wet Chemical Acid Digestion
18.4.1.3 Fusion Method
18.4.1.4 Dissolution and Extraction
18.4.1.5 Centrifugation
18.4.2 Sample Preparation for Liquid Samples
18.4.2.1 Filtration
18.4.2.2 Liquid-Liquid Extraction
18.4.2.3 Solid-Phase Extraction
18.4.2.4 Microextraction
18.4.2.5 Membrane Separation (Ultrafiltration/Dialysis)
18.5 Advancing Ion Chromatography: Unveiling Standardization, Validation, and Compliance Practices for Engaging Assays in Biological Matrices
18.6 Advanced Instrumentation in Ion-Exchange Chromatography: A Closer Look
18.6.1 Pump and Flow Regulator
18.6.2 Sample Injector
18.6.3 Column
18.6.4 Suppressor
18.6.5 Detector and Data Processor
18.7 Precision and Upkeep: Calibration and Maintenance in Ion Chromatography Instrumentation
18.8 Inorganic Ions: A Comprehensive Overview and Their Critical Role and Effect
18.8.1 Inorganic Cations
18.8.2 Inorganic Anions
18.9 Trends and Advances in the Detection of Inorganic Ions in Biological Matrices
18.10 Unveiling Inorganic Ions: Advanced Detection Techniques in Biological Matrices for Ion Chromatography
18.10.1 The Role of Ion Chromatography in Detecting Cations and Anions within Biological Matrix Analysis
18.11 Conclusions and Future Outlooks
References
19. Sample Preparation and Handling for Reliable Results
Virender, Rohit, Ashwani Kumar, Rakesh Kumar Gupta and Brij Mohan
19.1 Introduction
19.2 Solution Preparation and Concentration Expressions
19.2.1 Percentage Composition
19.2.2 Molarity
19.2.3 Molality
19.2.4 Normality
19.2.5 Parts Per Million/Billion (ppm/ppb)
19.2.6 Stock Solutions and Dilutions
19.3 Laboratory Facilities
19.3.1 Source of Water
19.3.2 Cleaning Facility
19.3.3 Steam Sterilization (Autoclave)
19.4 Introduction to Cell Culture
19.4.1 Growth Medium
19.4.2 Animal Cell Culture
19.4.2.1 Primary Cell Culture
19.4.2.2 Secondary Cell Culture
19.4.3 Microbial Culture
19.5 General Procedures for Sample Preparation
19.5.1 Liquid-Liquid Extraction (LLE)
19.5.2 Solid-Phase Extraction (SPE)
19.5.3 Protein Precipitation
19.5.4 Sample Loading and Elution
19.6 Analytical Chemistry Principles in Bioanalysis
19.6.1 Liquid Chromatography–Mass Spectroscopy (LC-MS)
19.6.1.1 Method Development Procedure
19.6.1.2 Method Optimization
19.6.1.3 Mode of Separation Technique
19.6.1.4 Selection of Stationary Phase/Column
19.6.1.5 Mobile Phase Selection
19.6.2 Capillary Electrophoresis
19.6.2.1 CE-MS for Bioanalysis of Drugs
19.6.2.2 CE-MS Coupling (Practical Considerations)
19.6.2.3 Sheath Liquid (Flow Rate and Composition)
19.6.2.4 Nebulizing Gas Pressure
19.6.2.5 Capillary Outlet Position
19.6.2.6 Sample Preparation
19.6.3 Toxicology Studies in Drug Metabolism Using LC-MS/MS
19.7 Key Findings, Challenges, and Conclusion
Acknowledgments
References
20. Data Analysis in Bioanalysis for Interpretation of Experimental Data
Jaymin Parikh, Keyur Bhatt, Krunal Modi, Jasbir Sangwan, Alexander A. Solovev and Brij Mohan
20.1 Introduction
20.2 Importance of Data Analysis
20.3 Types of Data in Bioanalysis
20.3.1 Qualitative Data in Bioanalysis
20.3.2 Quantitative Data in Bioanalysis
20.3.3 Complementary Nature of Qualitative and Quantitative Data
20.3.4 Challenges and Advances in Handling Both Types of Data
20.4 UV-Visible Spectroscopy Data for Bioanalysis
20.5 Fluorescence Spectroscopy Data for Bioanalysis
20.6 Mass Spectroscopy Data for Bioanalysis
20.7 Computational Tools for Data Analysis
20.8 Emerging Trends and Technologies in Bioanalysis: A Comprehensive Exploration
20.8.1 Single-Cell Analysis
20.8.2 Multiomics Integration
20.8.3 Artificial Intelligence (AI) and Machine Learning (ML) Integration
20.9 Challenges and Future Directions
20.10 Future Perspectives
Acknowledgments
References
21. Protein Identification Using Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry
Vipul D. Prajapati and Princy Shrivastav
21.1 Introduction
21.1.1 Overview of Mass Spectrometry in Proteomics
21.1.2 Brief History of MALDI Mass Spectrometry
21.2 Fundamentals of MALDI-MS
21.2.1 Principles of MALDI-MS
21.2.2 MALDI Sample Preparation Techniques
21.2.3 Instrumentation: Components and Operation
21.3 Sample Preparation for Protein Identification
21.3.1 Protein Extraction and Purification
21.3.2 Desalting and Concentration Methods
21.3.3 MALDI Matrix Selection and Optimization
21.4 MALDI-MS Data Acquisition
21.4.1 Ionization Process and Matrix Interactions
21.4.2 Mass Calibration and Spectral Acquisition
21.4.3 Data Processing (DP) and Signal-to-Noise Ratio (SNR) Enhancement
21.5 Database Searching and Protein Identification
21.5.1 Peptide Mass Fingerprinting
21.5.2 Tandem Mass Spectrometry (MS/MS) and Fragment Ion Analysis
21.5.3 Interpretation of Mass Spectra: Database Matching Algorithms
21.6 Challenges and Limitations
21.7 Applications and Case Studies
21.7.1 MALDI-MS in Clinical Proteomics
21.7.2 Protein Identification in Drug Discovery
21.7.3 Role of MALDI-MS in Biomarker Discovery
21.8 Advancements and Future Perspectives
21.8.1 Emerging Technologies and Methodologies
21.8.2 Integration with Other Omics Technologies
21.8.3 Potential for High-Throughput Proteomics
21.9 Conclusion
References
22. Applications of Electrothermal Atomic Absorption Spectrometry (ET-AAS) Toward Various Metal Analyses in Diverse Biological and Environmental Matrices
Aruna Jyothi Kora
22.1 Introduction
22.2 Electrothermal Atomic Absorption Spectrometry (ET-AAS)
22.2.1 Sample Introduction Techniques
22.2.2 Matrix Modifiers
22.2.3 Analyte Preconcentration Techniques
22.3 Conclusions
Acknowledgments
References
23. Thin-Layer Chromatography for Natural Product Analysis
Mahreen Imam, Syed Ali Raza Naqvi, Majid Muneer, Atta Ul Haq, Sadaf Ul Hassan,
Muhammad Rehan Hasan Shah Gilani, Naseem Abbas and Syeda Marab Saleem
23.1 Introduction
23.2 Natural Product and its Role in Human Civilization
23.3 Impact of Analytical Techniques in the Development of Natural Products
23.4 TLC for the Analysis of Natural Products
23.5 Theory and Working of TLC
23.5.1 Stationary Phases for TLC
23.5.2 Advances in TLC Stationary Phases
23.6 Mobile Phases for TLC
23.6.1 Aqueous Mobile Phases
23.6.2 Organic Modifier Mobile Phases
23.6.3 Mobile Phase Additives
23.7 Applicability of TLC in Screening of Natural Products
23.7.1 Using TLC to Examine Botanicals Samples for Analysis of Polyphenols
23.7.2 Screening Botanicals for Antimicrobial Properties Using TLC
23.7.3 TLC to Examine Botanicals Samples for Enzyme Inhibitors
23.7.4 TLC for Medicinal and Culinary Herb Screening
23.8 Advances in TLC
23.8.1 High-Performance TLC (HP-TLC)
23.8.2 TLC Coupled with Raman Spectroscopy
23.8.3 TLC in Densitometry Quantification
23.8.4 TLC Hyphenated with Matrix-Assisted Mass Spectrometry
23.9 Advanced TLC Systems
23.10 Miniaturization and Microfluidic TLC
23.11 Future Prospectus of TLC in the Advances of NPs
References
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