Targeting Galectins With Glycomimetics

被引:47
作者
Bertuzzi, Sara [1 ]
Quintana, Jon, I [1 ]
Arda, Ana [1 ]
Gimeno, Ana [1 ]
Jimenez-Barbero, Jesus [1 ,2 ,3 ]
机构
[1] CIC BioGUNE, Basque Res Technol Alliance, Derio, Spain
[2] Basque Fdn Sci, Ikerbasque, Bilbao, Spain
[3] Univ Basque Country UPV EHU, Fac Sci & Technol, Dept Organ Chem 2, Leioa, Spain
基金
欧洲研究理事会;
关键词
galectins; glycomimetics; glycans; molecular recogntion; drug design; CARBOHYDRATE-RECOGNITION DOMAIN; THOMSEN-FRIEDENREICH ANTIGEN; BOVINE SERUM-ALBUMIN; MOLECULAR-DYNAMICS; LINKER LENGTH; LUNG FIBROSIS; LECTIN; BINDING; DESIGN; AFFINITY;
D O I
10.3389/fchem.2020.00593
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Among glycan-binding proteins, galectins, beta-galactoside-binding lectins, exhibit relevant biological roles and are implicated in many diseases, such as cancer and inflammation. Their involvement in crucial pathologies makes them interesting targets for drug discovery. In this review, we gather the last approaches toward the specific design of glycomimetics as potential drugs against galectins. Different approaches, either using specific glycomimetic molecules decorated with key functional groups or employing multivalent presentations of lactose and N-acetyl lactosamine analogs, have provided promising results for binding and modulating different galectins. The review highlights the results obtained with these approximations, from the employment of S-glycosyl compounds to peptidomimetics and multivalent glycopolymers, mostly employed to recognize and/or detecthGal-1 andhGal-3.
引用
收藏
页数:17
相关论文
共 98 条
[1]   The recognition of glycans by protein receptors. Insights from NMR spectroscopy [J].
Arda, Ana ;
Jimenez-Barbero, Jesus .
CHEMICAL COMMUNICATIONS, 2018, 54 (38) :4761-4769
[2]   Peptides derived from human galectin-3 N-terminal tail interact with its carbohydrate recognition domain in a phosphorylation-dependent manner [J].
Berbis, M. Alvaro ;
Andre, Sabine ;
Canada, F. Javier ;
Pipkorn, Ruediger ;
Ippel, Hans ;
Mayo, Kevin H. ;
Kuebler, Dieter ;
Gabius, Hans-Joachim ;
Jimenez-Barbero, Jesus .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2014, 443 (01) :126-131
[3]   Clicked and long spaced galactosyl- and lactosylcalix[4]arenes: new multivalent galectin-3 ligands [J].
Bernardi, Silvia ;
Fezzardi, Paola ;
Rispoli, Gabriele ;
Sestito, Stefania E. ;
Peri, Francesco ;
Sansone, Francesco ;
Casnati, Alessandro .
BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY, 2014, 10 :1672-1680
[4]   Structural Basis for Distinct Binding Properties of the Human Galectins to Thomsen-Friedenreich Antigen [J].
Bian, Cheng-Feng ;
Zhang, Ying ;
Sun, Hui ;
Li, De-Feng ;
Wang, Da-Cheng .
PLOS ONE, 2011, 6 (09)
[5]   The neoglycoprotein mannose-bovine serum albumin, but not progesterone, activates T-type calcium channels in human spermatozoa [J].
Blackmore, PF ;
Eisoldt, S .
MOLECULAR HUMAN REPRODUCTION, 1999, 5 (06) :498-506
[6]   Galectin-1 inhibitors and their potential therapeutic applications: a patent review [J].
Blanchard, Helen ;
Bum-Erdene, Khuchtumur ;
Bohari, Mohammad Hussaini ;
Yu, Xing .
EXPERT OPINION ON THERAPEUTIC PATENTS, 2016, 26 (05) :537-554
[7]   Galectin-3 inhibitors: a patent review (2008-present) [J].
Blanchard, Helen ;
Yu, Xing ;
Collins, Patrick Michael ;
Bum-Erdene, Khuchtumur .
EXPERT OPINION ON THERAPEUTIC PATENTS, 2014, 24 (10) :1053-1065
[8]   Sequence-Defined Introduction of Hydrophobic Motifs and Effects in Lectin Binding of Precision Glycomacromolecules [J].
Boden, Sophia ;
Reise, Franziska ;
Kania, Jessica ;
Lindhorst, Thisbe K. ;
Hartmann, Laura .
MACROMOLECULAR BIOSCIENCE, 2019, 19 (04)
[9]  
Boecker Sophia, 2017, Bioengineering-Basel, V4, DOI 10.3390/bioengineering4020031
[10]   Galectin Binding to Neo-Glycoproteins: LacDiNAc Conjugated BSA as Ligand for Human Galectin-3 [J].
Boecker, Sophia ;
Laaf, Dominic ;
Elling, Lothar .
BIOMOLECULES, 2015, 5 (03) :1671-1696