Interaction of L-tryptophan with alpha-cyclodextrin: studies with calorimetry and proton nuclear magnetic resonance spectroscopy.

Abstract:

:The interaction of L-tryptophan with alpha-cyclodextrin was investigated in a 0.1 M phosphate buffer at pH 7.4 with a LKB 2277 microcalorimeter, using flow mixed mode at 25 degrees C. The thermodynamic parameters for inclusion complex formation obtained are as follows; DeltaG(0) = - 7.03 kJ/mol (K = 17.0), DeltaH(0) = - 9.50 kJ/mol, DeltaS(0) = - 8.3 J/mol K. The driving force for inclusion complex formation was considered to be mainly van der Waals-London dispersion force, and the contribution of hydrogen bonding was secondary in importance. Also, from the measurements of the proton nuclear magnetic resonance spectra and the model building with Corey-Pauling-Koltum atomic models, the probable structures of the complex, together with conformational change of L-tryptophan by complexation, were determined.

journal_name

J Pharm Sci

authors

Nishijo J,Tsuchitani M

doi

10.1002/1520-6017(200102)90:2<134::aid-jps4>3.0.co

subject

Has Abstract

pub_date

2001-02-01 00:00:00

pages

134-40

issue

2

eissn

0022-3549

issn

1520-6017

pii

S0022-3549(16)30711-0

journal_volume

90

pub_type

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