F.S. Nandel and H. Kaur, “Effect of terminal achiral and chiral residues on the conformational behaviour of poly ?zPhe and analysis of various interactions”, Indian Journal of Biochemistry and Biophysics, Vol. 40, No. 4, 2003, pp. 265-273.

has been cited by the following article:

• TITLE: Peptoids with aliphatic sidechains as helical structures without hydrogen bonds and collagen/ inverse-collagen type structures

  AUTHORS: Fateh S. Nandel, Avneet Saini

  KEYWORDS: Peptoids; Conformation; Helical Structure without Hydrogen Bonds; Collagen and Inverse-Collagen Type Structures

  JOURNAL NAME: Journal of Biophysical Chemistry, Vol.2 No.1, February 22, 2011

  ABSTRACT: Aliphatic homo-polypeptoids of NAla, NVal, NIle and NLeu both in the presence and absence of protecting groups adopt helical structures without hydrogen bonds with Φ, Ψ values of ~ 0, ± 90° with trans amide bonds. These structures are stabilized by carbonyl-carbonyl interactions and characterized by ~ 3.16 residues per turn with a pitch of ~ 6.13 Å. It has been shown that like polyvaline and polyleucine peptides, poly-peptoids can also be exploited for the construction of potential surfactant like molecules by incorporating charged amino acid residues at the N terminal. A single-handed template with Φ, Ψ values of ~ 0, 90° can be attained by incorporating L-leu or L-val at the C-terminal of poly-NIle. Analysis of the simulation results in water as a function of time reveals that the opening of helical structures without hydrogen bonds takes place at sub-picosecond time scale starting from the N-terminal. This leads to the formation of collagen or inverse-collagen type structures (Φ, Ψ ~ -60, 145° and 60, -145° respectively) stabilized by interactions of water molecules with the backbone carbonyl groups.