Trishomocubane amino acid as a β-turn scaffold
The synthesis and X-ray structure of two diasteriomeric heptapeptides [Ac-Ala-Ala-Ala-(R/S)-Cage-Ala-Ala-Ala-NH2] with a trishomocubane amino acid as a β-turn scaffold are reported. The amino acid was synthesized as a racemate and two diastereomeric peptides were obtained. The two peptides were sepa...
محفوظ في:
| المؤلفون الرئيسيون: | , , , , , , , , |
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| مؤلفون آخرون: | |
| التنسيق: | مقال |
| منشور في: |
2018
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| الموضوعات: | |
| الوصول للمادة أونلاين: | https://repository.li.mahidol.ac.th/handle/123456789/18979 |
| الوسوم: |
إضافة وسم
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| المؤسسة: | Mahidol University |
| الملخص: | The synthesis and X-ray structure of two diasteriomeric heptapeptides [Ac-Ala-Ala-Ala-(R/S)-Cage-Ala-Ala-Ala-NH2] with a trishomocubane amino acid as a β-turn scaffold are reported. The amino acid was synthesized as a racemate and two diastereomeric peptides were obtained. The two peptides were separated by preparative high-pressure liquid chromatography and crystals suitable for X-ray analysis were grown for both diasteriomeric peptides. In general, both the peptides satisfy the criteria for β-turn conformations. Five of the six Ala residues of both cage peptide crystals satisfy the criteria for 310-helix characteristics and the cage amino acid residue satisfied the α-helix classification. These experimental results confirm previous theoretical studies in our laboratory which predicted that the cage moiety would be a strong/active β-turn inducer. © 2008 The Authors. |
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