| People | Locations | Statistics |
|---|---|---|
| Naji, M. |
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| Motta, Antonella |
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| Aletan, Dirar |
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| Mohamed, Tarek |
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| Ertürk, Emre |
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| Taccardi, Nicola |
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| Kononenko, Denys |
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| Petrov, R. H. | Madrid |
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| Alshaaer, Mazen | Brussels |
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| Bih, L. |
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| Casati, R. |
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| Muller, Hermance |
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| Kočí, Jan | Prague |
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| Šuljagić, Marija |
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| Kalteremidou, Kalliopi-Artemi | Brussels |
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| Azam, Siraj |
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| Ospanova, Alyiya |
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| Blanpain, Bart |
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| Ali, M. A. |
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| Popa, V. |
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| Rančić, M. |
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| Ollier, Nadège |
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| Azevedo, Nuno Monteiro |
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| Landes, Michael |
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| Rignanese, Gian-Marco |
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Spiliopoulou, Maria
University of Patras
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (7/7 displayed)
- 2021High-throughput macromolecular polymorph screening via an NMR and X-ray powder diffraction synergistic approach: the case of human insulin co-crystallized with resorcinol derivativescitations
- 2020Insulin polymorphism induced by two polyphenols: new crystal forms and advances in macromolecular powder diffractioncitations
- 2019Unit-cell response of tetragonal hen egg white lysozyme upon controlled relative humidity variationcitations
- 2019Revisiting the structure of a synthetic somatostatin analogue for peptide drug designcitations
- 2018<i>In situ</i>detection of a novel lysozyme monoclinic crystal form upon controlled relative humidity variationcitations
- 2017Dengue virus 3 NS5 methyltransferase domain: expression, purification, crystallization and first structural data from microcrystalline specimenscitations
- 2016Coxsackievirus B3 protease 3C: expression, purification, crystallization and preliminary structural insightscitations
Places of action
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article
Revisiting the structure of a synthetic somatostatin analogue for peptide drug design
Abstract
<jats:p>Natural or artificially manufactured peptides attract scientific interest worldwide owing to their wide array of pharmaceutical and biological activities. X-ray structural studies are used to provide a precise extraction of information, which can be used to enable a better understanding of the function and physicochemical characteristics of peptides. Although it is vulnerable to disassociation, one of the most vital human peptide hormones, somatostatin, plays a regulatory role in the endocrine system as well as in the release of numerous secondary hormones. This study reports the successful crystallization and complete structural model of octreotide, a stable octapeptide analogue of somatostatin. Common obstacles in crystallographic studies arising from the intrinsic difficulties of obtaining a suitable single-crystal specimen were efficiently overcome as polycrystalline material was employed for synchrotron and laboratory X-ray powder diffraction (XPD) measurements. Data collection and preliminary analysis led to the identification of unit-cell symmetry [orthorhombic, <jats:italic>P</jats:italic>2<jats:sub>1</jats:sub>2<jats:sub>1</jats:sub>2<jats:sub>1</jats:sub>, <jats:italic>a</jats:italic> = 18.5453 (15), <jats:italic>b</jats:italic> = 30.1766 (25), <jats:italic>c</jats:italic> = 39.798 (4) Å], a process which was later followed by complete structure characterization and refinement, underlying the efficacy of the suggested (XPD) approach.</jats:p>