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Conformations of hydrophobic peptides in trifluoroethanol, water and in solid state: A circular dichroism and Fourier Transform Infrared study

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Title Conformations of hydrophobic peptides in trifluoroethanol, water and in solid state: A circular dichroism and Fourier Transform Infrared study
 
Creator Jagannadham, Medicharala V
Krishnamurthy, Akella S R
Husain, Sajid
Nagaraj, Ramakrishnan
 
Description 422-428
The conformations of peptides corresponding to
KLLIALVLCFLPLAALG have been examined in trifluoroethanol (TFE), aqueous medium
by circular dichroism spectroscopy and in the solid state by Fourier
Transform Infra Red Spectroscopy (FTIR). The l7-residue parent peptide and
peptides corresponding to shorter segments LVLCFLPLAALG and CFLPLAALG showed
preference for helical conformation in TFE. Even the shorter hydrophobic
peptides corresponding to KLLIA and LVL showed propensity for β-turn conformations
in TFE. However, peptides corresponding to the relatively polar segment
FLPLAALG were unordered in TFE. In water, peptides that showed ordered conformation
in TFE preferred β-conformation. In solid-state, FTIR spectra indicated that
the hydrophobic peptides adopt β -structures with extensive hydrogen bond network
in the solid state. The hydrophobic core segment thus appears to dictate the
conformational propensity of the peptide.
 
Date 2012-12-31T20:06:51Z
2012-12-31T20:06:51Z
1999-12
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15473
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.36(6) [December 1999]