Carbohydrate-Based Therapeutics E-Book
142,99 €
Mehr erfahren.
- Herausgeber: Wiley-VCH GmbH
- Kategorie: Wissenschaft und neue Technologien
- Sprache: Englisch
The book covers current progress and opens new frontiers in carbohydrate-based therapeutic applications. It presents a detailed background of the diseases coupled with the subsequent carbohydrate-based therapies. This aspect renders this book unique and will serve as a quick reference practical book of carbohydrate applications. The link between chemistry and design of novel carbohydrate-based medicines is highlighted and broad overview of all the potential applications of carbohydrates is given. Emphasis is laid on concepts used for carbohydrate drug design, structure-activity relationship and impact on health and diseases.
Sie lesen das E-Book in den Legimi-Apps auf:
Seitenzahl: 753
Veröffentlichungsjahr: 2023
Ähnliche
Table of Contents
Cover
Table of Contents
Title Page
Copyright
Dedication
Foreword
Acknowledgments
1 Antibacterial Carbohydrate Vaccines
1.1 Introduction
1.2 Carbohydrate-Based Vaccines
1.3 Components of Glycoconjugate Vaccines
1.4 Technologies Employed for Production of Glycoconjugate Vaccines
1.5 Conclusion
Acknowledgments
References
2 Antifungal Glycoconjugate Vaccines
2.1 Human Fungal Infections
2.2 Immunity Against Fungal Pathogens
2.3 Carbohydrate Antigens in Fungal Cell Wall
2.4 Glycoconjugate Vaccines Against
Candida albicans/Candida auris
2.5 Glycoconjugate Vaccines Against
Cryptococcus neoformans
2.6 Glycoconjugate Vaccines Against
Aspergillus fumigatus
2.7 Universal Fungal Polysaccharide Antigens
2.8 Conclusions and Future Prospects
References
3 Carbohydrate-Based Antiviral Vaccines
3.1 Introduction
3.2 Human Immunodeficiency Virus
3.3 Influenza A Virus
3.4 Hepatitis C Virus
3.5 Ebola Virus
3.6 SARS-CoV-2 Virus
3.7 Conclusions and Outlook
Acknowledgments
References
4 Bacterial Glycolipid Lipid As and Their Potential as Adjuvants
4.1 Introduction
4.2 Bacterial Glycolipid Lipid A: an Innate Immune Stimulant
4.3 Vaccines Containing Natural LPS as Adjuvants
4.4 LPS and Lipid A in the Environment or Fermented Foods as Adjuvants
4.5 Synthetic and Semisynthetic Lipid As as Adjuvants
4.6 Developing Novel Lipid A Adjuvants
4.7 Symbiotic Bacterial Lipid As
4.8 Lipid A-Based Self-Adjuvanting Vaccines
4.9 Conclusions
References
5 Antiadhesive Carbohydrates and Glycomimetics
5.1 Introduction
5.2 DC-SIGN-Mediated Viral Adhesion and Entry into Myeloid Cells
5.3 The Bacterial Adhesin FimH
5.4
Pseudomonas aeruginosa
Virulence Factors (PA-IL and PA-IIL)
5.5 General Aspects
References
6 Targeting Carbohydrates in Cancer – Analytical and Biotechnological Tools
6.1 Aberrant Protein Glycosylation in Cancer
6.2 Detection and Mapping of Carbohydrate-Based Antigens in Human Neoplastic Tissues
6.3 Imaging Mass Spectrometry
6.4
In Situ
Proximity Ligation Assay
6.5 Glycan Microarrays
6.6 Glycoengineered
In Vitro
,
In Vivo
, and
Ex Vivo
Models
6.7 Structural Elucidation of Glycoconjugates: Glycomic and Glycoproteomic Strategies
6.8 Concluding Remarks
List of Abbreviations
References
7 Carbohydrate-Specific Monoclonal Antibody Therapeutics
7.1 Introduction
7.2 Types of Monoclonal Antibodies
7.3 Humanization of Monoclonal Antibodies
7.4 Breakthrough Research
7.5 mAbs from Preclinical to Clinical Studies
7.6 Globo Series
7.7 New Treatment Options for Neuroblastoma
7.8 Summary
List of Abbreviations
References
8 Carbohydrates in Tissue Engineering
8.1 Introduction
8.2 Biomaterials and Medical Devices: Natural and Synthetic Strategies
8.3 Carbohydrates in Animal-Derived Medical Devices: Friends or Foes?
8.4 Glycoengineering Application to Regenerative Medicine
8.5 Future Opportunities and Major Challenges
Conflict of Interest
References
9 Carbohydrate-Based Therapeutics for Lysosomal Storage Disorders
9.1 An Introduction to Lysosomal Storage Disorders (LSDs)
9.2 Available Treatments for LSDs: The Role of Carbohydrate-Based Therapeutics
9.3 Mucopolysaccharidoses
9.4 Sphingolipidoses
9.5 Glycogen Storage Disorders
9.6 Glycoproteinoses
9.7 Conclusions
Acknowledgments
Abbreviations and Acronyms
References
10 Carbohydrates and Carbohydrate-Based Therapeutics in Alzheimer's Disease
10.1 Introduction
10.2
O
-GlcNAc Transferase (OGT) and
O
-GlcNAc Hydrolase (OGA) in Neurodegeneration
10.3 GalNAc in Neurodegeneration
10.4 Chitosan and Derivatives in AD Brain
10.5 Cholinesterase Inhibitors
10.6 Fyn Kinase Inhibitors
10.7 Amyloid Protein–Protein Interaction Inhibitors
10.8 Inhibitors of Aβo and/or Oxidative Stress-Induced Neurotoxicity
10.9 Carbohydrate–Protein Interactions as Potential Therapeutic Targets Against AD
10.10 Conclusion
List of Abbreviations
Acknowledgments
References
11 Carbohydrate-Based Antithrombotics
11.1 Introduction
11.2 Antithrombotic Drugs
11.3 Heparin
11.4 Mechanism of Interaction with Coagulation Factors
11.5 Low Molecular Weight Heparins
11.6 Drugs Based on Natural GAG Mixtures
11.7 Defibrotide
11.8 Pentosan Polysulfate
11.9 Fondaparinux and Related Synthetic Oligosaccharides
11.10 Chemoenzymatic Synthesis of Oligosaccharides
11.11 Conclusions and Perspectives
Acknowledgment
References
Index
End User License Agreement
List of Tables
Chapter 1
Table 1.1 List of glycoconjugate vaccines licensed by FDA
a
for use in the US...
Table 1.2 Chemical structure of CPS repeating units within serogroups
or
typ...
Chapter 2
Table 2.1 Main advantages and disadvantages of potential treatments for syst...
Chapter 3
Table 3.1 Significant examples of synthetic 2G12 epitope mimics.
Chapter 5
Table 5.1 Carbohydrate epitopes used by bacteria for colonization and entry ...
Table 5.2 Overview over multivalent systems employed for DC-SIGN targeting....
Chapter 8
Table 8.1 Examples of commercial heparin-coating technologies.
Table 8.2 Examples of commercial medical devices and formulations produced f...
Chapter 9
Table 9.1 Lysosomal storage disorders object of this chapter, classified acc...
Table 9.2 Classification of the mucopolysaccharidoses (MPS) and available ER...
Table 9.3 Pharmacological chaperones for MPSs.
Table 9.4 Inhibitors of IDS and GALNS (human enzymes).
Table 9.5 PCs and combined ERT/PC for Fabry disease.
Table 9.6 PCs for Gaucher disease.
Table 9.7 PCs for GM1 gangliosidosis and Morquio B disease.
Table 9.8 PCs for GM2 gangliosides.
Table 9.9 Inhibitors of GALC.
Table 9.10 ERT for Pompe disease.
Table 9.11 PCs for Pompe disease.
Table 9.12 PCs for α-mannosidosis
Chapter 10
Table 10.1 Inhibition constant of compounds
23a
–
23i
over OGA and HEXB.
Table 10.2 Pharmacodynamic of brain
O
-GlcNac protein in rats treated with th...
Table 10.3 Inhibition constants of compounds
62a–62g
for hOGA and lyso...
Table 10.4
K
i
values for hOGA and
β
HexB,
K
i
selectivity ratios of inhib...
Table 10.5 Inhibition data of hOGA and lysosomal hexosaminidases (HexA/B) by...
Table 10.6 Data obtained in assays to determine the inhibition of hOGA, the ...
Table 10.7 Inhibition (%) of BChE for different concentrations of the compou...
Table 10.8 Inhibitory constant
K
i
for nucleosides
99–123
as determined...
Chapter 11
Table 11.1 Average molecular weight (
M
w
) and polydispersity degree (D), anti...
List of Illustrations
Chapter 1
Figure 1.1 Immune response following immunization with polysaccharides (a) a...
Figure 1.2 Representative examples of homo- and heterobifunctional linkers f...
Figure 1.3 Summary of the technologies employed for glycoconjugate productio...
Figure 1.4 The protein glycan coupling technology (PGCT): schematic illustra...
Chapter 2
Figure 2.1 Schematic representation of carbohydrates in fungal cell walls....
Figure 2.2 Vaccine candidates against
Candida
infections.
Figure 2.3 Vaccine candidates against
Cryptococcus neoformans
.
Figure 2.4 Vaccine candidates against
Aspergillus fumigatus
.
Chapter 3
Scheme 3.1 Conjugation reactions and linker chemistry applied in the synthes...
Figure 3.1 Synthetic 2G12 bnAb epitope mimics.
Scheme 3.2 Synthesis of unnatural C6-methylated mannose and assembly of a no...
Scheme 3.3 Chemoenzymatic synthesis of V1V2 glycopeptides.
Scheme 3.4 Chemical synthesis of V1V2 glycopeptide.
Figure 3.2 Synthetic V3-directed bnAb epitope mimics.
Figure 3.3 Antigen–α-GalCer prodrug conjugate vaccine against influenza chal...
Figure 3.4 Glycofullerene “superballs” substituted with up to 120 mannose un...
Chapter 4
Figure 4.1
E. coli
LPS and Kdo-lipid A.
Figure 4.2 Chemical structure of 3D-MPL and lipid IVa.
Figure 4.3 Innate immune system activation via TLR4/MD2.
Figure 4.4 Molecular mechanism of TLR4/MD2 dimerization.
Figure 4.5 Chemical structures of various lipid As and lipid A analogs.
Figure 4.6 Chemical structures of various lipid As.
Figure 4.7 RC-529.
Figure 4.8 Chemical structures of parasitic bacterial LPS partial structures...
Figure 4.9 Chemical structures of
A. faecalis
LOS structures.
Figure 4.10 Chemical structures of synthesized
A. faecalis
lipid As.
Figure 4.11 Self-adjuvanting strategy.
Figure 4.12 Chemical structures of adjuvant–antigen complexes. (a) MPL conju...
Chapter 5
Figure 5.1 Structure of DC-SIGN. (a) Schematic depiction of DC-SIGN domain o...
Figure 5.2 Monovalent carbohydrate derivatives and glycomimetics as DC-SIGN ...
Scheme 5.1 Synthesis of α-1,2-mannobiose mimetics. (a) MCPBA, rt; (b) Cu(OTf...
Figure 5.3 Representative structures of pseudo-dimannoside glycomimetics and...
Figure 5.4 Structure of Polyman26 (
13
).
Figure 5.5 Structure of glycomimetic
14
and its multivalent presentation.
Figure 5.6 Schematic representation of FimH–uroplakin Ia (UP1a) interactions...
Figure 5.7 “Open” (left) and “closed” (right) conformation of the tyrosine g...
Figure 5.8 Structures of potent FimH antagonists and representative optimiza...
Figure 5.9 Crystal structures of PA-IL and PA-IIL in complex with
D
-galactos...
Figure 5.10 Representative structures of mono- and oligovalent PA-IL antagon...
Figure 5.11 Representative structures of PA-IIL antagonists (
6-11
) and bifun...
Chapter 6
Figure 6.1 Biotechnological and analytical tools for the identification, fun...
Chapter 7
Figure 7.1 Difference in structure between subclasses of IgGs [5–7].
Figure 7.2 Chemical structure of glycolipid disialoganglioside (GD2) [83, 84...
Figure 7.3 Illustration of mechanisms for GD2 antibody-targeted destruction ...
Figure 7.4 Illustration of potential immune responses to neuroblastoma tumor...
Chapter 8
Figure 8.1 Examples of polysaccharides expressed in human tissues.
Figure 8.2 Hyaluronic acid benzyl ester.
Figure 8.3 Examples of nonhuman polysaccharides employed for biomedical devi...
Figure 8.4 Xenoantigens responsible for immunoresponse in humans.
Figure 8.5 (a) Metabolic incorporation of Ac5ManNTGc in the sialic acid path...
Chapter 9
Figure 9.1 Comparison of a healthy lysosome with a defective one of LSD pati...
Figure 9.2 Cartoon representing the Pharmacological Chaperone (PC) concept....
Figure 9.3 Structures of iminosugars involved in ERT, SRT, and PCT for LSDs....
Chapter 10
Figure 10.1 Healthy neuron vs. neuron after degeneration.
Figure 10.2 Illustration of
O
-GlcNAc modification of proteins via
O
-GlcNAc t...
Figure 10.3 Illustration of amyloidogenic and non-amyloidogenic cleavage of ...
Figure 10.4 Structure of selected OGA inhibitors.
Figure 10.5 Mechanism for hOGA inhibition. (a) Mechanism proposed by Macaule...
Scheme 10.1 The first synthesis of PUGNAc by Beer et al. [45, 46]. Reagents/...
Scheme 10.2 Improved approach to prepare PUGNAc by Vasella and Mohan [48]. R...
Scheme 10.3 Synthesis of PUGNAc and
N
-acylated derivatives as reported by St...
Scheme 10.4 PUGNAc synthesis developed by Goddard-Borger and Stubbs [50]. Re...
Scheme 10.5 Synthesis of PUGNAc and representative analogs with modified car...
Figure 10.6 Structure of PUGNAc, nagstatin, and GlcNAcstatins designed and t...
Scheme 10.6 The first synthesis of GlcNAcstatin [52]. Reagents/solvent and y...
Scheme 10.7 Preparation of GlcNAcstatin and analogs [59]. Reagents/solvent a...
Scheme 10.8 Synthesis of thiazoline-based OGA inhibitors
62a
–
62g
as reported...
Scheme 10.9 Synthesis of Thiamet-G developed by Yuzwa et al. [61] Reagents/s...
Scheme 10.10 Preparation of Thiamet-G-based thiazoline inhibitors
65
and
66a
Figure 10.7 Structure of 5-substituted methyl tetrahydropyranothiazole compo...
Scheme 10.11 Synthesis of MK8719 [67]. Reagents/solvent and yield: (a) Boc
2
O...
Scheme 10.12 Synthesis of the N
9
and N
7
nucleosides
92
and
93
, respectively....
Scheme 10.13 Synthesis of the (6′
S
)- and (6′
R
)-configurated N
7
nucleosides
9
...
Scheme 10.14 Synthesis of the N
9
and N
7
nucleosides
99
to
122
as reported by...
Figure 10.8 Simplified illustration of Aβo-induced Fyn activation leading to...
Scheme 10.15 Synthesis of saracatinib (
123
) [102]. Reagents/solvent and yiel...
Figure 10.9 Structure of Fyn kinase inhibitor
134
and of the inhibitors of A...
Scheme 10.16 Synthesis of per-O-methylated
C
-glucosyl polyphenols
133–135
...
Scheme 10.17 Synthesis of per-O-methylated
C
-glucosyl polyphenols [103]. Rea...
Figure 10.10 Two major processes to be targeted by amyloid protein–protein i...
Figure 10.11 Amyloid anti-aggregation agents (
141
,
142
) and Aβo-PrP
C
disrupt...
Scheme 10.18 Flavone synthesis as described by Marta et al. [106–108] Reagen...
Scheme 10.19 Synthesis of
C
-glucosyl flavones as described by Matos et al. [...
Scheme 10.20 Synthesis of resveratrol 2-deoxyglycosides with neuroprotective...
Figure 10.12 Polyphenol structures: resveratrol glycosides
150, 151
, glucosy...
Scheme 10.21 The first synthesis of glucosylresveratrol
152
[112]. Reagents/...
Chapter 11
Figure 11.1 Structures of the prevailing (a) and minor (b) heparin disacchar...
Figure 11.2 Structural differences associated with different conformations o...
Figure 11.3 A simplified diagrammatic representation of the classical blood ...
Figure 11.4 Heparin-antithrombin-thrombin (a) and pentasaccharide-antithromb...
Guide
Cover
Title Page
Copyright
Dedication
Foreword
Acknowledgments
Table of Contents
Begin Reading
Index
End User License Agreement
Pages
iii
iv
v
xv
xvi
xvii
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39
40
41
42
43
44
45
46
47
48
49
50
51
52
53
54
55
56
57
58
59
60
61
62
63
64
65
66
67
68
69
70
71
72
73
74
75
76
77
78
79
80
81
82
83
84
85
86
87
88
89
90
91
92
93
94
95
96
97
98
99
100
101
102
103
104
105
106
107
108
109
110
111
112
113
114
115
116
117
118
119
120
121
122
123
124
125
126
127
128
129
130
131
132
133
134
135
136
137
138
139
140
141
142
143
144
145
146
147
148
149
150
151
152
153
154
155
156
157
158
159
160
161
162
163
164
165
166
167
168
169
170
171
172
173
174
175
176
177
178
179
180
181
182
183
184
185
186
187
188
189
190
191
192
193
194
195
196
197
198
199
200
201
202
203
204
205
206
207
208
209
210
211
212
213
214
215
216
217
218
219
220
221
223
224
225
226
227
228
229
230
231
232
233
234
235
236
237
238
239
240
241
242
243
245
246
247
248
249
250
251
252
253
254
255
256
257
258
259
260
261
262
263
264
265
266
267
268
269
270
271
272
273
274
275
276
277
278
279
280
281
282
283
284
285
286
287
288
289
290
291
292
293
294
295
296
297
298
299
300
301
302
303
304
305
306
307
308
309
310
311
312
313
314
315
316
317
318
319
320
321
322
323
324
325
326
327
328
329
330
331
332
333
334
335
336
337
338
339
340
341
342
343
344
345
346
347
348
349
350
351
352
353
354
355
356
357
358
359
360
361
362
363
364
365
366
367
368
369
370
371
372
373
374
375
376
377
378
379
380
381
382
383
384
385
386
387
388
389
390
391
Carbohydrate-Based Therapeutics
Edited by Roberto Adamo and Luigi Lay
Editors
Dr. Roberto AdamoGlaxoSmithKlineResearch CenterVia Fiorentina 153100 SienaItaly
Prof. Luigi LayUniversity of MilanDepartment of ChemistryVia Golgi 1920133 MilanItaly
Cover Images: © daniskg/Pixabay; © Linnas/Shutterstock; © sefa ozel/E+/Getty Images
All books published by WILEY-VCH are carefully produced. Nevertheless, authors, editors, and publisher do not warrant the information contained in these books, including this book, to be free of errors. Readers are advised to keep in mind that statements, data, illustrations, procedural details or other items may inadvertently be inaccurate.
Library of Congress Card No.: applied for
British Library Cataloguing-in-Publication Data:A catalogue record for this book is available from the British Library.
Bibliographic information published by the Deutsche NationalbibliothekThe Deutsche Nationalbibliothek lists this publication in the Deutsche Nationalbibliografie; detailed bibliographic data are available on the Internet at <http://dnb.d-nb.de>.
© 2024 WILEY-VCH GmbH, Boschstraße 12, 69469 Weinheim, Germany
All rights reserved (including those of translation into other languages). No part of this book may be reproduced in any form – by photoprinting, microfilm, or any other means – nor transmitted or translated into a machine language without written permission from the publishers. Registered names, trademarks, etc. used in this book, even when not specifically marked as such, are not to be considered unprotected by law.
Print ISBN: 978-3-527-34870-1ePDF ISBN: 978-3-527-83131-9ePub ISBN: 978-3-527-83133-3oBook ISBN: 978-3-527-83132-6
In the memory of Veronica, wife and mother of my beloved children
Luigi Lay
In the memory of Raffaele, my father. Smell of lead and freshly printed books in his typography
Roberto Adamo
Foreword
Glycans are ubiquitous in nature, and in animal and human biology, they make up an average of 10% of cell membranes as proteoglycans, glycoproteins, and glycolipids and being attached to over 50% of proteins in the cell. Thus, it is not surprising that glycoconjugates have become an important facet of modern molecular medicine, with increasing recognition of the key roles they play in health and disease, ranging from nutrition, microbiomes, and natural aging processes to congenital disorders of glycosylation, inflammation, immune response, cancer, and microbial infections. Modern analytical, synthetic, and biochemical tools in the glycosciences have provided a deep structural and mechanistic insight into the complex functions of glycans, and this complexity can now be addressed by computational methods including modeling and machine learning. There are already small-molecule glycan derivatives in the clinic, such as the iminosugars miglustat and miglitol, but the most prominent success stories have been in biopharmaceuticals. Many of them are glycoconjugates, including carbohydrate-based vaccines against pneumonia and other infectious diseases, glycoproteins including hEPO and many therapeutic antibodies. This book provides the reader with an insight into some of the most topical applications of glycans in medicine.
The carbohydrate coats of microbes are highly diverse, and fungal and bacterial cell surface polysaccharides and viral glycoproteins present distinct microbe-specific targets for vaccination strategies. The chapter by Del Bino et al. reviews antifungal glycoconjugate vaccines in clinical development. Since polysaccharides are T-cell-independent antigens, long-lasting immune responses are achieved by conjugation of the polysaccharide epitope to carrier peptides and proteins. Complementary approaches include immunostimulatory adjuvants, and the use of the bacterial glycolipid Lipid A as adjuvants is discussed in the chapter by Shimoyama and Fukase. Given the potential toxic side effects of Lipid A, they discuss how an understanding of detailed structure–function relationships will be essential to develop effective analogues that are suitable in the clinic. Carbohydrate-based vaccines are relevant to many antimicrobial strategies, and Compostella et al. review the state-of-art of antibacterial vaccines, and Plata et al. discuss antiviral vaccines. With the current challenges presented to society by increasing resistance against many antimicrobial compounds, these vaccination strategies promise to be effective alternatives to fight infections both in humans and animals.
By understanding the biological function of cell-surface polysaccharides in animals and microbes, scientists can also use these glycans for biomedical applications. Two examples are discussed in the chapters by Russo et al. and by Cramer et al. Polysaccharides can be used as key components in tissue engineering, using their biocompatible and biodegradable properties as surface molecules. This has important applications in medical devices and regenerative medicine. Another interesting application of polysaccharides is in anti-adhesives for new therapeutic approaches to antimicrobials as discussed by Cramer et al.
In humans, glycan structures are very canonical with highly conserved biosynthetic pathways defining the different glycan structures such as lipids, N- and O-glycans, and proteoglycans. Diversity comes with misregulation of these pathways, resulting in over or under-expression of glycan motifs. We now understand that the resulting disorders of glycosylation can be either genetic or also observed in many diseases. Matassini et al. review therapeutic approaches to one class of congenital disorders of glycosylation, Lysosomal Storage Diseases, which are a group of metabolic disorders leading to accumulation of unmetabolized substrates in the lysosomes and subsequent cell dysfunction. Particularly promising therapeutic candidates are iminosugars, a class of small-molecule drugs initially designed as target enzyme transition state inhibitors.
Aberrant changes in glycosylation are also hallmarks of many diseases, in particular in diverse cancers. Duarte et al. review the analytical tools that allow for the identification of tumor-associated carbohydrate antigens in patient samples, resulting in new biomarkers for cancer progression. Andreana et al. review anti-cancer therapeutic monoclonal antibodies targeting glycans expressed on tumor cells. However, cancer is not the only disease hallmarked by mis-glycosylation and as one further example Matos et al. discuss carbohydrate-based therapeutic targets in Alzheimer’s disease, including the role that dysregulation of O-GlcNAcs plays in formation of protein aggregates. Bisio et al. focus on the use of heparin-like glycosaminoglycans, as powerful drugs for prevention of thrombosis.
In conclusion, this book provides an authoritative introduction to the roles of glycan-based diagnostics and therapeutics and is written by leading experts in the field both from industry and academia. The book will be of great interest to glyco-scientists by bringing together such a diverse set of topics. It should also convince a much broader community of scientists looking for new diagnostic tools and therapies in challenging diseases such as cancer that glycans have become an essential part of modern molecular medicine.
Sabine L. Flitsch
MIB & School of Chemistry, The University of Manchester, United Kingdom
Acknowledgments
We are glad that this project is finally coming to light. There is a plethora of books dealing with advancements in carbohydrate chemistry applied to biological challenges. However, our project aims at differing from all those publications as we wished to start from disease areas which need to be tackled in order to impact on health of millions of patients to highlight the modern tools that carbohydrate and glycoconjugate chemistry can nowadays offer.
We acknowledge all authors who kindly contributed to make this book possible, and Prof. S. Flitsch for providing an excellent preface to the chapters.
We are hopeful that this book can attract the interest of the broadly interdisciplinary scientific community around the glycoscience world. Most importantly, we hope it can be useful not only to senior scientists and specialized professionals from both industry and academy, but also to inspire students and young researchers who will form the next generation of glycoscientists.
Roberto Adamo and Luigi Lay
