1225014-70-9Relevant academic research and scientific papers
Switching the H-bonding network of a foldamer by modulating the backbone chirality and constitutional ratio of amino acids
Ramesh, Veera V. E.,Vijayadas, Kuruppanthara N.,Dhokale, Snehal,Gonnade, Rajesh G.,Rajamohanan, Pattuparambil R.,Sanjayan, Gangadhar J.
supporting information, p. 7072 - 7075 (2013/10/22)
This communication describes the folding propensity of a heterofoldamer motif featuring proline (Pro) and anthranilic acid (Ant) residues in a 1:2:1 (α:β:α) constitutional ratio. Structural investigations unequivocally suggest that the hydrogen-bonding network of this foldamer motif can be switched between 9-membered and 6-membered by modulating the backbone chirality and constitutional ratio of the amino acid residues.
A synthetic zipper peptide motif orchestrated via co-operative interplay of hydrogen bonding, aromatic stacking, and backbone chirality
Nair, Roshna V.,Kheria, Sanjeev,Rayavarapu, Suresh,Kotmale, Amol S.,Jagadeesh, Bharatam,Gonnade, Rajesh G.,Puranik, Vedavati G.,Rajamohanan, Pattuparambil R.,Sanjayan, Gangadhar J.
, p. 11477 - 11480 (2013/09/02)
Here, we report on a new class of synthetic zipper peptide which assumes its three-dimensional zipper-like structure via a co-operative interplay of hydrogen bonding, aromatic stacking, and backbone chirality. Structural studies carried out in both solid- and solution-state confirmed the zipper-like structural architecture assumed by the synthetic peptide which makes use of unusually remote inter-residual hydrogen-bonding and aromatic stacking interactions to attain its shape. The effect of chirality modulation and the extent of noncovalent forces in the structure stabilization have also been comprehensively explored via single-crystal X-ray diffraction and solution-state NMR studies. The results highlight the utility of noncovalent forces in engineering complex synthetic molecules with intriguing structural architectures.
