Peripheral cyclic beta-amino acids balance the stability and edge-protection of beta-sandwiches
Engineering water-soluble stand-alone beta-sandwich mimetics is a current challenge because of the difficulties associated with tailoring long-range interactions. In this work, single cis-(1R,2S)-2-aminocyclohexanecarboxylic acid mutations were introduced into the edge strands of the eight-stranded...
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| Dokumentumtípus: | Cikk |
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Royal Society of Chemistry Publishing
2018
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| Sorozat: | ORGANIC & BIOMOLECULAR CHEMISTRY
16 No. 30 |
| doi: | 10.1039/c8ob01322e |
| mtmt: | 3399101 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/13944 |
| LEADER | 02132nab a2200265 i 4500 | ||
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| 100 | 1 | |a Olajos Gábor | |
| 245 | 1 | 0 | |a Peripheral cyclic beta-amino acids balance the stability and edge-protection of beta-sandwiches |h [elektronikus dokumentum] / |c Olajos Gábor |
| 260 | |a Royal Society of Chemistry Publishing |c 2018 | ||
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| 490 | 0 | |a ORGANIC & BIOMOLECULAR CHEMISTRY |v 16 No. 30 | |
| 520 | 3 | |a Engineering water-soluble stand-alone beta-sandwich mimetics is a current challenge because of the difficulties associated with tailoring long-range interactions. In this work, single cis-(1R,2S)-2-aminocyclohexanecarboxylic acid mutations were introduced into the edge strands of the eight-stranded beta-sandwich mimetic structures from the betabellin family. Temperature-dependent NMR and CD measurements, together with thermodynamic analyses, demonstrated that the modified peripheral strands exhibited an irregular and partially disordered structure but were able to exert sufficient shielding on the hydrophobic core to retain the predominantly beta-sandwich structure. Although the frustrated interactions decreased the free energy of unfolding, the temperature of the maximum stabilities increased to or remained at physiologically relevant temperatures. We found that the irregular peripheral strands were able to prevent edge-to-edge association and fibril formation in the aggregation-prone model. These findings establish a beta-sandwich stabilization and aggregation inhibition approach, which does not interfere with the pillars of the peptide bond or change the net charge of the peptide. | |
| 700 | 0 | 1 | |a Hetényi Anasztázia |e aut |
| 700 | 0 | 1 | |a Wéber Edit |e aut |
| 700 | 0 | 1 | |a Szögi Titanilla |e aut |
| 700 | 0 | 1 | |a Fülöp Lívia |e aut |
| 700 | 0 | 1 | |a Martinek Tamás |e aut |
| 856 | 4 | 0 | |u http://publicatio.bibl.u-szeged.hu/13944/1/c8ob01322e.pdf |z Dokumentum-elérés |