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Conformational study of N-methylated alanine peptides and design of A<img src='/image/spc_char/beta.gif' border=0> inhibitor

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Title Conformational study of N-methylated alanine peptides and design of A inhibitor
 
Creator Nandel, Fateh S
Jaswal, Radhika R
 
Subject Conformation
N-Methylated alanine peptides
Molecular simulations
Helical structure without hydrogen bond
Carbonyl-carbonyl interactions
Aβ inhibitor design
 
Description 7-18
N-Methylation increases
the proteolytic stability of peptides and leads to improved pharmacological and
increased nematicidal property against plant pathogens. In this study, the
quantum mechanical and molecular dynamic simulation approaches were used to
investigate conformational behavior of peptides containing only N-methylated
alanine (NMeAla) residues and N-methylated alanine and alanine residues at
alternate positions. The amide bond geometry was found to be trans
and the poly NMeAla peptides were shown to populate in the helical
structure without hydrogen bond with
,
values of ~ 0, 90˚ stabilized by carbonyl-carbonyl interactions. Molecular
dynamic simulations in water/methanol revealed the formation of β-strand
structure, irrespective of the starting geometry due to the interaction of
solvent molecules with the carbonyl groups of peptide backbone. Analysis of
simulation results as a function of time suggested that the opening of helical
structure without hydrogen bond started from C-terminal. Conformational behavior of peptides containing
N-MeAla and Ala
was used to design Ab peptide inhibitor and the model tetrapeptide Ac-Ala-NMeAla-Ala-NHMe in the
β-strand structure was shown to interact with the hydrophobic stretch of
Aβ15-42 peptide.
 
Date 2014-03-03T17:52:41Z
2014-03-03T17:52:41Z
2014-02
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/27293
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.51(1) [February 2014]