Record Details

Effects of salt and denaturant on structure of the amino terminal alpha-helical segment of an antibacterial peptide dermaseptin and its binding to model membranes

NOPR - NISCAIR Online Periodicals Repository

View Archive Info
 
 
Field Value
 
Title Effects of salt and denaturant on structure of the amino terminal alpha-helical segment of an antibacterial peptide dermaseptin and its binding to model membranes
 
Creator Thennarasu, Sathiah
Nagaraj, Ramakrishnan
 
Description 142-148
The amino terminal 1-18 domain of dermaseptin s is an
important determinant of its structure as well as the antibacterial activity. A
thorough investigation on the structure of the 18-residue peptide (DI8) and its
binding to model membranes in presence of salt and denaturant guanidinium
chloride has been carried out. In presence of salt, there is an increase in the

fraction of peptide molecules in helical conformation.
In presence of the denaturant, D18 is unordered, but addition of the structure-promoting
solvent trifluoroethanol results in a transition to the helical conformation. In
presence of denaturant, the peptide is unordered, but binding to lipid vesicles
is not abolished. Investigation of model membrane permeabilizing ability

of the peptide in solutions containing various
proportions of sodium chloride and guanidinium chloride indicates th at vesicle
permeabilization parallels extent of binding. The peptide thus binds to lipid
vesicles in an unfolded state. Since the peptide has propensity to fold into a
helical conformation, lipid induced transition to a helical structure occurs,
followed by membrane

permeabilization as a result of pore formation.
 
Date 2012-12-24T18:37:00Z
2012-12-24T18:37:00Z
2001-06
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15285
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.38(3) [June 2001]