Structural and physical–chemical evaluation of bradykinin potentiating peptide and its high soluble supramolecular complex.
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Date
2010
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Abstract
The supramolecular interactions between a
Bradykinin Potentiating Peptide (BPP10c) and b-cyclodextrin
(bCD) have been investigated by using several
techniques. These new properties acquired by the inclusion
phenomena are important in developing a strategy for
pharmaceutical formulation. The BPP10c structural elucidation
and its inclusion complex formed have been investigated
using Nuclear Magnetic Resonance techniques. The
peptide secondary structure was investigated using infrared
spectroscopy in solution, Circular Dichroism and NMR. In
addition, the thermodynamic parameters of the inclusion
process were also evaluated using Isothermal Titration
Calorimetry. The results obtained by these physical–
chemical techniques suggested a 1:1 complex formed by
interaction between the Tryptophan amino acid residue and
the bCD cavity. The peptide secondary structure was not
substantially modified for the inclusion process. In addition,
the inclusion process proved to be spontaneous
(DG8 = -2.53 kcal mol-1), with an enthalpy reduction
(DH8 = -3.72 kcal mol-1) and a favored entropic variation
(TDS8 = -1.19 kcal mol-1).
Description
Keywords
Peptides, Bradykinin potentiating peptides, Supramolecular complexes, Intermolecular interactions
Citation
SOUSA, F. B. de et al. Structural and physical–chemical evaluation of bradykinin potentiating peptide and its high soluble supramolecular complex. Journal of Inclusion Phenomena and Macrocyclic Chemistry, v. 67, p. 407-422, 2010. Disponível em: <https://link.springer.com/article/10.1007/s10847-009-9723-6>. Acesso em: 16 jan. 2018.