doctoral dissertation
Povzetek
This thesis principally focuses on the development of glycomimetic ligands with improved affinity to Siglec-8. Siglec-8 is a member of the Siglec family, I-type lectins that contain a sialic acid-binding domain and that play different roles in cell-cell interactions and cell signaling. Siglec-8 is a CD33- related protein expressed exclusively on mast cells and eosinophils, and weakly on basophils. Crosslinking of Siglec-8 with antibodies leads to apoptosis of eosinophils and inhibition of degranulation of mast cells. Apoptosis has also been induced when eosinophils were treated with a glycopolymer (6’-sulfo-sLex-polyacrylamide polymer). Therefore, Siglec-8 represents a very interesting new pharmacological target for the treatment of eosinophil- or mast cell-associated diseases, such as asthma, chronic rhinosinusitis, chronic urticaria, hypereosinophilic syndromes, mast cell and eosinophil malignancies, and eosinophilic gastrointestinal disorders. Recently, the NMR solution structure of the Siglec-8 lectin domain was solved in complex with its preferred ligand, the tetrasaccharide 6′-sulfo sialyl Lewisx (Neu5Acα2-3[6S]Galβ1-4[Fucα1-3]GlcNAc). The main interactions involve a salt bridge between Arg109 and the carboxylate of sialic acid and a second salt bridge between Arg56 and Gln59 and the sulfate at the 6-position of the galactose moiety. Interestingly, the sulfate plays a key role in both binding and specificity to Siglec-8. In addition, hydrogen bonds exist between hydroxyl groups 7, 8 and 9 of sialic acid and Tyr7, Ser118 and Gln122. In contrast, the fucose and glucosamine subunits show only minor interactions. This led to the suggestion that the disaccharide substructure 6-sulfo-Sia-Gal might represent the minimal binding epitope for Siglec-8.
Ključne besede
Ni podatka o ključnih besedah
Podatki
Jezik: |
Angleški jezik |
Leto izida: |
2022 |
Tipologija: |
2.08 - Doktorska disertacija |
Organizacija: |
UL FFA - Fakulteta za farmacijo |
Založnik: |
[B. M. Girardi] |
UDK: |
615.4:54:576.36(043.3) |
COBISS: |
105504003
|
Št. ogledov: |
13 |
Št. prenosov: |
2 |
Ocena: |
0 (0 glasov) |
Metapodatki: |
|
Ostali podatki
Sekundarni jezik: |
Slovenski jezik |
Sekundarni povzetek: |
Ta doktorska naloga se osredotoča predvsem na razvoj glikomimetičnih ligandov z izboljšano afiniteto do Siglec-8. Siglec-8 je član družine Siglec, lektinov tipa I, ki vsebujejo domeno, ki veže sialično kislino, in imajo različne vloge pri interakcijah med celicami in celični signalizaciji. Siglec- 8 je CD33 sorodni protein, izražen izključno v tkivnih bazofilcih (mastocitih) in eozinofilcih, šibko pa v bazofilcih. Povezovanje Siglec-8 s protitelesi vodi do apoptoze eozinofilcev in zaviranja degranulacije mastocitov. Apoptoza se je pojavila tudi pri tretiranju eozinofilcev z glikopolimerom (6'-sulfo-sLex-poliakrilamidnim polimerom). Zato Siglec-8 predstavlja zelo zanimivo novo farmakološko tarčo za zdravljenje bolezni, povezanih z eozinofilci ali mastociti, kot so astma, kronični rinosinuzitis, kronična urtikarija, hipereozinofilni sindromi, malignosti mastocitov in eozinofilcev ter eozinofilne gastrointestinalne motnje. Pred kratkim so razrešili NMR strukturo lektinske domene Siglec-8 v kompleksu s svojim ligandom tetrasaharidnim 6'-sulfo sialil Lewisx (Neu5Acα2-3[6S]Galβ1-4[Fucα1-3]GlcNAc). Glavne interakcije vključujejo solni most med Arg109 in karboksilatom sialične kisline ter drugi solni most med Arg56 in Gln59 ter sulfatom na mestu 6 galaktoznega dela. Zanimivo je, da ima sulfat ključno vlogo pri vezavi in specifičnosti na Siglec-8. Poleg tega obstajajo vodikove vezi med hidroksilnimi skupinami 7, 8 in 9 sialične kisline ter Tyr7, Ser118 in Gln122. Nasprotno pa podenote fukoze in glukozamina tvorijo le šibkejše interakcije. To je pripeljalo do predloga, da bi disaharidna podstruktura 6-sulfo-Sia-Gal lahko predstavljala minimalni vezavni epitop za Siglec-8. |
Sekundarne ključne besede: |
ligandi;Siglec-8;Farmacevtska kemija;Disertacije;Apoptoza; |
Vrsta dela (COBISS): |
Doktorska disertacija |
Strani: |
221 str. |
ID: |
17698417 |