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Late-stage thiazole functionalization towards novel Galectin-1 inhibitors

Weber, Emil August LU (2026) KEMP30 20252
Department of Chemistry
Abstract
Based on a previously published thiazole-containing glycomimetic, that works as an inhibitor to
human galectin-1 novel compounds where synthesized to serve as binders to the same protein.
Functionalization was achieved through electrophilic substitution on the thiazole ring using a
range of different electrophiles. Characterization via NMR spectroscopy revealed a reactantbased
regioselectivity between functionalization on the carbon-5 – predominantly for sulphurbased
electrophiles – or nitrogen-3 – for carbon-based electrophiles – of the thiazole ring.
Molecular dynamic simulations confirm that both isomers are capable of binding in a pocket that
remained unoccupied with their precursor. FP binding-assays produced Kd values of up to... (More)
Based on a previously published thiazole-containing glycomimetic, that works as an inhibitor to
human galectin-1 novel compounds where synthesized to serve as binders to the same protein.
Functionalization was achieved through electrophilic substitution on the thiazole ring using a
range of different electrophiles. Characterization via NMR spectroscopy revealed a reactantbased
regioselectivity between functionalization on the carbon-5 – predominantly for sulphurbased
electrophiles – or nitrogen-3 – for carbon-based electrophiles – of the thiazole ring.
Molecular dynamic simulations confirm that both isomers are capable of binding in a pocket that
remained unoccupied with their precursor. FP binding-assays produced Kd values of up to
0.78 μM. While the binding affinity of the precursor could not be surpassed the successful
functionalization provides a pathway towards improved inhibitors. (Less)
Popular Abstract
Galectin-1 is a protein found in humans and other mammals. It is involved in a variety of bodily
functions. Previous studies on mice have shown that reducing the activity of this protein can
reduce the growth of tumors. To achieve this, small molecules can be designed that bind to the
protein and thereby deactivate it. In this project I have designed and produced several new
molecules of this kind by adding a new segment to an existing one, hoping to improve on its
properties. By analysing the exact structure of these new molecules, I found out, that depending
on the composition of the new segment it attached itself on one of two different parts of the
molecule. Lastly, I tested how good my new molecules bind to the protein and... (More)
Galectin-1 is a protein found in humans and other mammals. It is involved in a variety of bodily
functions. Previous studies on mice have shown that reducing the activity of this protein can
reduce the growth of tumors. To achieve this, small molecules can be designed that bind to the
protein and thereby deactivate it. In this project I have designed and produced several new
molecules of this kind by adding a new segment to an existing one, hoping to improve on its
properties. By analysing the exact structure of these new molecules, I found out, that depending
on the composition of the new segment it attached itself on one of two different parts of the
molecule. Lastly, I tested how good my new molecules bind to the protein and found that, while
none could surpass the old one they came close enough to make it worthwhile to try new variants
of them in the future. Since new segments could be introduced at two different regions of the
molecule, this opens up two new ways to find molecules which can fight cancer. (Less)
Please use this url to cite or link to this publication:
author
Weber, Emil August LU
supervisor
organization
course
KEMP30 20252
year
type
L3 - Miscellaneous, Projetcs etc.
subject
keywords
organic chemistry, glycomimetics, thiazole derivatives
language
English
id
9222213
date added to LUP
2026-02-11 11:41:45
date last changed
2026-02-11 11:41:45
@misc{9222213,
  abstract     = {{Based on a previously published thiazole-containing glycomimetic, that works as an inhibitor to
human galectin-1 novel compounds where synthesized to serve as binders to the same protein.
Functionalization was achieved through electrophilic substitution on the thiazole ring using a
range of different electrophiles. Characterization via NMR spectroscopy revealed a reactantbased
regioselectivity between functionalization on the carbon-5 – predominantly for sulphurbased
electrophiles – or nitrogen-3 – for carbon-based electrophiles – of the thiazole ring.
Molecular dynamic simulations confirm that both isomers are capable of binding in a pocket that
remained unoccupied with their precursor. FP binding-assays produced Kd values of up to
0.78 μM. While the binding affinity of the precursor could not be surpassed the successful
functionalization provides a pathway towards improved inhibitors.}},
  author       = {{Weber, Emil August}},
  language     = {{eng}},
  note         = {{Student Paper}},
  title        = {{Late-stage thiazole functionalization towards novel Galectin-1 inhibitors}},
  year         = {{2026}},
}