Special Issue "Glycosaminoglycans and Their Mimetics"


A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Molecular Diversity".

Deadline for manuscript submissions: closed (31 December 2014)

Special Issue Editor

Guest Editor
Dr. Vito Ferro
School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia
Website: http://staff.scmb.uq.edu.au/staff/vito-ferro
E-Mail: v.ferro@uq.edu.au
Interests: carbohydrate chemistry; medicinal chemistry; heparanase inhibitors; heparan sulfate mimetics

Special Issue Information

Dear Colleagues,

Glycosaminoglycans (GAGs) are linear, polyanionic polysaccharide chains with enormous structural diversity that are usually found attached to a protein core to form proteoglycans. The GAG chains are composed of repeating disaccharide subunits containing a uronic acid (D-GlcA or L-IdoA) or hexose (D-Gal) linked to a hexosamine (D-GlcNAc or D-GalNAc). There are five distinct types of GAGs: heparan sulfate (HS), chondroitin sulfate (CS), dermatan sulfate (DS), keratan sulfate (KS) and hyaluronic acid (HA). GAGs are found on the surface of every mammalian cell and in the extracellular matrix and mediate numerous biological and pathological processes by interacting with various proteins (e.g., growth factors, cytokines, proteases, glycosidases and many others). Apart from their roles in normal growth and development, GAGs have attracted much interest because of the important roles they play in diseases such as cancer and inflammation and in infectious diseases where they are used as entry receptors by some viruses. The well-known heparin, a highly sulfated form of HS, has of course been used as an anticoagulant drug for decades. In more recent times, low molecular weight heparins (LMWH) and fondaparinux, the antithrombin-binding pentasaccharide sequence found in heparin, have complemented the use of unfractionated heparin as anticoagulant drugs.
There has been considerable interest in understanding the precise nature of the interactions between GAGs and their binding partners, in particular to define which specific sequences (or arrangement of domains) are responsible for biological activity. Advances in analytical techniques such as NMR and MS to identify GAG sequences and the synthesis of defined, homogeneous GAG oligosaccharides and glycoconjugates for use in biological studies will play an important role in advancing our understanding in this area. The development of GAG mimetics is also of great interest, particularly for the discovery of new therapeutics. GAG mimetics are compounds that block GAG–protein interactions and, by so doing, can interfere with disease processes. Activity in this area has been greatest in the field of cancer where several compounds have entered the clinic, with one of them (PI-88) in Phase III trials.
We invite our colleagues to submit research articles and comprehensive reviews addressing the above mentioned and related topics for publication in this Special Issue.

Dr. Vito Ferro
Guest Editor


Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed Open Access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs).


  • heparan sulfate
  • heparin
  • LMWH
  • chondroitin sulfate
  • dermatan sulfate
  • hyaluronic acid
  • glycosaminoglycan
  • proteoglycan
  • heparanase

Published Papers (2 papers)

Download All Papers
Sort by:
Display options:
Select articles Export citation of selected articles as:
Select/unselect all
Displaying article 1-2
p. 1626-1642
by , , , ,  and
Molecules 2015, 20(1), 1626-1642; doi:10.3390/molecules20011626
Received: 28 November 2014 / Accepted: 29 December 2014 / Published: 19 January 2015
Show/Hide Abstract | PDF Full-text (7626 KB)
(This article belongs to the Special Issue Glycosaminoglycans and Their Mimetics)
p. 608-624
by , ,  and
Molecules 2015, 20(1), 608-624; doi:10.3390/molecules20010608
Received: 30 October 2014 / Accepted: 26 December 2014 / Published: 5 January 2015
Show/Hide Abstract | PDF Full-text (1465 KB) | Supplementary Files
(This article belongs to the Special Issue Glycosaminoglycans and Their Mimetics)
abstract graphic
Select/unselect all
Displaying article 1-2
Select articles Export citation of selected articles as:

Last update: 10 July 2014

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert