Study of the BPP7a peptide and its β-cyclodextrin complex: physicochemical characterization and complete sequence specific NMR assignments
The BPP7a heptapeptide, p-Glu¹Asp²Gly³Pro4Ile5Pro6Pro7, forms an association complex with β-cyclodextrin in a 1:1 molar ratio. The peptide and its complex were characterized by circular dichroism (CD) and isothermal titration calorimetry (ITC), which showed a very weak interaction between the β-cyclodextrin and the peptide. Assignments of all hydrogen resonances of the peptide alone and as a complex were made using ¹H nuclear magnetic resonance (NMR) experiments at 400 and 600 MHz. High resolution diffusion ordered spectroscopy (HR-DOSY) experiments were carried out to establish the self-aggregation state of BPP7a. It was also shown that the β-cyclodextrin breaks the molecular clusters leading to complex formation. In addition, the anti-hypertensive activity of the BPP7a/β-cyclodextrin complex was evaluated in spontaneous hypertensive rats (SHR), showing increased activity compared to that of pure BPP7a.
| Main Authors: | , , , , , , |
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| Format: | Digital revista |
| Language: | English |
| Published: |
Sociedade Brasileira de Química
2011
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| Online Access: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532011000900020 |
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