Advances in Glycosaminoglycans (GAGs) and Mimetics

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Chemical Biology".

Deadline for manuscript submissions: 31 March 2026 | Viewed by 16

Special Issue Editors


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Guest Editor
Department of Chemistry, University of North Texas, Dallas, TX, USA
Interests: application of GAGs and GAG mimetics in thrombopoiesis, thrombosis, and inflammation; studies of GAG-protein interactions; photoaffinity labeling technology
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Special Issue Information

Dear Colleagues,

Research involving glycosaminoglycans (GAGs), negatively charged biomacromolecules, has gained prominence in recent years. This is in part due to advances in the field, particularly with respect to their isolation, chemical and enzymatic synthesis, and structural characterization. Furthermore, the field has seen an increase in the number of tools available to study the interactions of these molecules with their protein targets, with computational approaches becoming more routine given the challenges with obtaining GAGs in pure form and the increased access to high computing power. The development of molecules that mimic the structure and function of natural GAGs is also witnessing an upsurge. These molecules, which are touted to be easier to synthesize/prepare and be more homogenous, are in some instances thought to be superior to their parent molecules in terms of function. 

Considering the vast potential of GAGs and their mimetics as well as the challenges associated with GAG research, the advancements in this field deserve special attention. As suggested by the title, this Special Issue encompasses fundamental science discoveries and applications of GAGs and GAG-like molecules and will cover topics on (1) the synthesis/preparation of GAGs and GAG-like molecules, (2) the structural characterization of GAGs and GAG-like molecules, (3) the interaction of GAGs and GAG-like molecules with cellular targets, and (4) therapeutic and other applications of GAGs and GAG-like molecules. 

Dr. Daniel Afosah
Dr. Rami A. Al-Horani
Guest Editors

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Keywords

  • glycosaminoglycans (GAGs)
  • hyaluronan
  • heparin
  • chondroitin sulfate
  • keratan sulfate
  • dermatan sulfate
  • sulfation
  • GAG mimetics
  • GAG-binding proteins

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Published Papers (1 paper)

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Review

16 pages, 805 KiB  
Review
Heparin, Heparin-like Molecules, and Heparin Mimetics in Breast Cancer: A Concise Review
by Diego R. Gatica Portillo, Yishu Li, Navneet Goyal, Brian G. Rowan, Rami A. Al-Horani and Muralidharan Anbalagan
Biomolecules 2025, 15(7), 1034; https://doi.org/10.3390/biom15071034 - 17 Jul 2025
Abstract
Heparin and heparan sulfate are essential in various biological processes relevant to cancer biology and pathology. Given the clinical importance of breast cancer, it is of high interest to seek more effective and safer treatment. The application of heparins (UFH, LMWH, ULMWH, fondaparinux) [...] Read more.
Heparin and heparan sulfate are essential in various biological processes relevant to cancer biology and pathology. Given the clinical importance of breast cancer, it is of high interest to seek more effective and safer treatment. The application of heparins (UFH, LMWH, ULMWH, fondaparinux) and heparin mimetics as potential treatments is particularly interesting. Their use led to promising results in various breast cancer models by exhibiting anti-angiogenic and anti-metastatic properties. This article concisely reviews studies involving heparins and mimetics in both in vitro and in vivo breast cancer settings. We highlight molecules, conjugates, delivery systems, and combinations involving heparin or its mimetics. We also survey several potential biological targets such as VEGF, FGF-2, TGFβ-1, PDGF-B, NPP-1, CXCL12-CXCR4 axis, and CCR7-CCL21 axis. Overall, heparins and their mimetics, conjugates, and combinations represent a powerful strategy to effectively and safely treat breast cancer, which is the most common cancer diagnosed in women worldwide and the fifth leading cause of cancer-related deaths worldwide. Full article
(This article belongs to the Special Issue Advances in Glycosaminoglycans (GAGs) and Mimetics)
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