Peptide applications in biomedicine, biotechnology and bioengineering / edited by Sotirios Koutsopoulos.

Format:

Book

Contributor:

Koutsopoulos, Sotirios, editor.

Series:

Woodhead Publishing series in biomaterials.

Woodhead Publishing Series in Biomaterials

Language:

English

Subjects (All):

Peptides--Laboratory manuals.

Peptides.

Physical Description:

1 online resource (640 pages) : illustrations.

Edition:

1st ed.

Place of Publication:

Duxford, England : Woodhead Publishing, 2018.

Summary:

Peptide Applications in Biomedicine, Biotechnology and Bioengineering summarizes the current knowledge on peptide applications in biomedicine, biotechnology and bioengineering. After a general introduction to peptides, the book addresses the many applications of peptides in biomedicine and medical technology. Next, the text focuses on peptide applications in biotechnology and bioengineering and reviews of peptide applications in nanotechnology. This book is a valuable resource for biomaterial scientists, polymer scientists, bioengineers, mechanical engineers, synthetic chemists, medical doctors and biologists. Presents a self-contained work for the field of biomedical peptides Summarizes the current knowledge on peptides in biomedicine, biotechnology and bioengineering Covers current and potential applications of biomedical peptides

Contents:

Front Cover

“Peptide Applications in Biomedicine, Biotechnology and Bioengineering

Copyright Page

Contents

List of contributors

1 Peptide synthesis: Methods, trends, and challenges

1.1 Introduction

1.2 Solid phase peptide synthesis

1.3 Solid supports (resins and linkers)

1.3.1 Resins

1.3.2 Linkers for Fmoc-based SPPS

1.4 Protecting groups

1.4.1 Nα amino protecting groups

1.4.2 Side-chain protecting groups

1.5 Coupling reagents

1.6 Deprotection: Cleavage solutions

1.7 Microwave-assisted solid-phase peptide synthesis

1.8 Green peptide synthesis

1.9 Future challenges: Conclusions

References

2 Synthetic approaches of naturally and rationally designed peptides and peptidomimetics

2.1 Natural and rationally designed peptides

2.1.1 Cyclic peptides

2.1.2 Disulfide-rich peptides

2.1.2.1 Conotoxins

2.1.2.2 Cyclotides

2.1.3 Cyclodepsipeptides

2.1.3.1 "Head-to-tail" cyclodepsipeptides

2.1.3.2 "Head-to-side-chain" cyclodepsipeptides

2.1.4 Lantibiotics

2.1.5 Stapled peptides

2.2 Peptidomimetics

2.2.1 Peptoids and Peptoid derivatives

2.2.2 AA-peptides

2.2.3 Azapeptides

2.2.4 Urea-based peptidomimetics

2.2.5 Nonpeptide-based peptidomimetics

Acknowledgments

3 Applications of de novo designed peptides

3.1 Introduction

3.2 Peptide building blocks

3.2.1 α-Helices, helical bundles, and coiled coils

3.2.1.1 α-Helices

3.2.1.2 Coiled coils

3.2.1.3 Helical bundles

3.2.2 β-Strands and sheets

3.2.2.1 β-Strands

3.2.2.2 β-Sheets

3.2.3 Collagens

3.3 De novo designed peptide structures and their applications

3.3.1 Tissue engineering and regeneration

3.3.1.1 Scaffolds from self-assembled β-structured components

3.3.1.2 SAFs (self-assembling fibers) from α-helical building blocks.

3.3.1.3 Tissue engineering and regeneration with collagen-mimetic peptides

3.3.1.4 Short peptide motifs as molecular signals

3.3.2 Drug encapsulation, release, and delivery

3.3.2.1 Drug encapsulation and release from hydrogels

3.3.2.2 Discrete structures for encapsulation, release, and delivery

3.3.2.3 Translocating and permeating peptides for drug delivery

3.3.3 Antigen display and vaccine development

3.3.4 Membrane protein stabilization

3.3.4.1 α-Helical amphipathic peptides

3.3.4.2 Short, self-assembling peptides

3.3.5 Imaging contrast agents

3.3.5.1 Translocating and targeting peptide conjugates

3.3.5.2 De novo designed chelating peptides

3.3.6 3D printing-peptide bioinks

3.3.7 Nanoparticle and nanowire synthesis

3.3.7.1 Peptide-directed nanoparticle synthesis

3.3.7.2 Nanowire synthesis

3.4 Conclusions and outlook

3.5 Summary of de novo designed peptides

4 Design and applications of cyclic peptides

4.1 Introduction

4.2 Cyclic peptides in nature

4.3 Types of cyclic peptides: classification

4.3.1 Size

4.3.2 Number of rings

4.3.3 Physical properties

4.3.4 Type of cyclization

4.3.5 Type of building blocks

4.3.6 Type of secondary structure

4.4 Methods for the design of cyclic peptides

4.5 Approaches to the preparation of CPs

4.6 Limitations of cyclic peptides

4.7 Applications of cyclic peptides

4.8 Concluding remarks

Further reading

5 Peptides containing D-amino acids and retro-inverso peptides: General applications and special focus on antimicrobial pep...

5.1 Introduction and overview

5.2 Designing D-AAs containing peptides

5.3 General applications of D-AAs containing peptides

5.4 AMPs as promising bioinspired molecules

5.5 AMPs partially constituted of D-AAs (diastereomeric AMPs).

5.6 All-D-amino acid AMPs

5.7 Retro-inverso AMPs

5.8 Future trends and biomedical applications

6 Peptide nutraceuticals

6.1 Introduction

6.2 Antioxidant peptides

6.3 Antihypertensive peptides

6.4 Anticancer/antiproliferative peptides

6.5 Antiinflammatory peptides

6.6 Antimicrobial peptides

6.7 Future prospectives

7 Peptoid applications in biomedicine and nanotechnology

7.1 Introduction

7.2 Synthesis and functional properties of peptoids

7.2.1 Solid-phase synthesis of sequence-specific peptoids

7.2.2 Solution polymerization of polypeptoids

7.2.3 Secondary structure in sequence-specific peptoids

7.2.4 Physical properties of peptoids

Crystallization behavior of peptoids

Thermal-responsive properties of polypeptoids

7.3 Applications in biomedicine and nanotechology

7.3.1 Combinatorial libraries for peptoid ligand screening for therapeutics

7.3.2 Peptoids for antifouling coating applications

7.3.3 Peptoids for antimicrobial application

7.3.4 Peptoids as antifungal agents

7.3.5 Peptoids as anticancer drugs

7.3.6 Peptoid-modulated crystal growth for biominerals and antifreeze agents

7.3.7 Peptoid architectures for biomimetic materials research

7.3.8 Peptoids for delivery of nucleic acids

7.3.9 Peptoids as collagen mimetics

7.3.10 Nanostructure based on self-assembly of peptoids

Nanostructures based on self-assembly of peptoids in bulk

Nanostructures based on the solution self-assembly of peptoids

7.3.11 Polyethylene glycol mimetic peptoids for biopharmaceuticals

7.3.12 Simulation of peptoid architectures

8 Peptides as therapeutics

8.1 The role of natural peptides in the body

8.2 Where peptide therapeutics fit in the spectrum between small molecules and proteins.

8.3 The limitations of peptides as therapeutics

8.4 Efforts to overcome peptide limitations

8.5 Conclusion

9 Peptides for biopharmaceutical applications

9.1 Introduction

9.2 Incentives for the use of peptides as biopharmaceutical products

9.2.1 Structural properties of peptides

9.2.2 Potency and selectivity

9.2.3 Tolerable ADME-Tox profile

9.2.4 Low bioaccumulation

9.2.5 Increased probability of regulatory approval

9.3 Challenges to the use of peptides as biopharmaceutics

9.3.1 Poor in vivo stability

9.3.2 Poor oral bioavailability

9.3.3 Low membrane permeability

9.3.4 Poor solubility

9.3.5 Possibilities of undesired immunogenic responses

9.4 State-of-the-art techniques for overcoming the aforementioned challenges

9.4.1 Peptide engineering via amino acid substitution

9.4.2 Peptide conjugation

9.4.3 Hydrocarbon stapling

9.4.4 Novel formulation and alternate delivery strategies

9.4.5 Strategies for targeted delivery of peptide biopharmaceuticals

9.4.6 Strategies for peptide-assisted transdermal drug delivery

9.5 Future outlook

10 Host defense (antimicrobial) peptides

10.1 Overview of host defense peptides

10.2 General features of HDPs

10.3 Host defense peptides as immunomodulators

10.3.1 Effects of HDPs on inflammatory responses

10.3.2 HDPs can exhibit direct chemoattractant activity

10.3.3 HDPs promote wound healing and angiogenesis

10.3.4 The roles of HDPs in autophagy, apoptosis, and oxidative stress

10.3.5 Modulation of the adaptive immune response by HDPs

10.4 Direct antimicrobial activities of HDPs

10.4.1 Bacterial cell membrane disruption by HDPs

10.4.2 Inhibition of cell wall formation by HDPs

10.4.3 Antimicrobial HDPs targeting intracellular processes

10.5 Methods of bacterial resistance to HDPs.

10.5.1 Bacterial surface remodeling to inhibit binding

10.5.2 Active efflux and degradation of HDPs

10.5.3 Additional HDP resistance mechanisms

10.6 Antibiofilm activities of HDPs

10.6.1 Biofilm prevention using peptide-coated surfaces

10.7 Designing novel HDPs

10.7.1 Template-based design

10.7.2 Structure-guided design

10.7.3 Computational modeling of HDPs

10.8 The future of HDPs: From the bench to the clinic

10.8.1 Current commercialization challenges and potential solutions

10.8.2 Final thoughts

Abbreviations

11 Peptides in immunoengineering

11.1 Introduction

11.1.1 Progress and challenges in engineering immunity

11.1.1.1 Key cellular actors in the immune system

11.1.2 Peptides in immunoengineering

11.2 Peptides as antigens: Immunogenic peptides to engineer immune responses

11.2.1 Considerations for the design of peptide antigens

11.2.1.1 Choosing the peptide antigen

11.2.1.2 Improving the peptide antigen

11.2.2 Peptide antigens modulating immune responses

11.3 "Active" peptides: Peptides with a function

11.3.1 Targeting peptides

11.3.1.1 Targeting the innate immune system

11.3.1.2 Targeting the adaptive immune system

11.3.1.3 Targeting antigen-presenting cells

11.3.1.4 Other targeting peptides in immune engineering

11.3.2 Enzyme cleavable peptides for immunoengineering

11.4 Peptides in supramolecular structures

11.4.1 Advantages of supramolecular assembly for immunological applications

11.4.2 Peptide assemblies

11.4.2.1 Assembly of peptides into fibers

11.4.2.2 Conjugated peptide assemblies

11.4.3 Further delivery strategies

11.4.3.1 Virus-like particles

11.4.3.2 Encapsulation of peptides in nanoparticle assemblies

11.4.4 Future directions

12 Peptide-based vaccines.

12.1 Types of vaccines.

Notes:

Includes bibliographical references and index.

Description based on online resource; title from PDF title page (EBC, viewed November 28, 2017).

ISBN:

0-08-100736-1

0-08-100742-6