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Right-handed 14-Helix in β3-Peptides from L-Aspartic Acid Monomers by Kamaljit Kaur; Tara Sprules; Wael Soliman; Reem Beleid; Sahar Ahmed is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Right-handed 14-Helix in β3-Peptides from L-Aspartic Acid Monomers about?

beta-Peptides made from L-aspartic acid monomers form a new class of beta 3-peptides. Here we report the first three-dimensional NMR solution structure of a beta 3-hexapeptide (1) from L-aspartic acid monomers in 2,2,2-trifluoroethanol (TFE). We show that 1 forms a right-handed 14-helical structure in TFE. alpha-peptides from naturally occurring L-amino acids adopt a right-handed alpha-helix whereas beta 3-peptides formed from beta 3-amino acids derived from naturally occurring L-amino acids form left-handed 14-helices. The right-handed 14-helical conformation of 1 is a better mimic of alpha-peptide conformations. Using the NMR structure of 1 in TFE, we further study the conformation of 1 in water, as well as two similar beta 3-peptides (2 and 3) in water and TFE by molecular dynamics (MD) simulations. NMR and MD results suggest loss of secondary structure of 1 in water and show that it forms a fully extended structure. 2 and 3 contain residues with oppositely charged side chains that engage in salt-bridge interactions and dramatically stabilize the 14-helical conformation in aqueous media.

Who reads Right-handed 14-Helix in β3-Peptides from L-Aspartic Acid Monomers?

Author

Kamaljit Kaur; Tara Sprules; Wael Soliman; Reem Beleid; Sahar Ahmed

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1570-9639)

Published

2008

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)