@article { ISI:000323019400017,
	title = {Synthetic zipper peptide motif orchestrated via co-operative interplay of hydrogen bonding, aromatic stacking, and backbone chirality},
	journal = {Journal of the American Chemical Society},
	volume = {135},
	number = {31},
	year = {2013},
	month = {AUG},
	pages = {11477-11480},
	publisher = {AMER CHEMICAL SOC},
	address = {1155 16TH ST, NW, WASHINGTON, DC 20036 USA},
	abstract = {<p>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.</p>},
	issn = {0002-7863},
	doi = {10.1021/ja405455g},
	author = {Nair, Roshna V. and Kheria, Sanjeev and Rayavarapu, Suresh and Kotmale, Amol S. and Jagadeesh, Bharatam and Gonnade, Rajesh G. and Puranik, Vedavati G. and Rajamohanan, Pattuparambil R. and Sanjayan, Gangadhar J.}
}
@article { ISI:000343985600001,
	title = {Synthetic turn mimetics and hairpin nucleators: quo vadimus?},
	journal = {Chemical Communications},
	volume = {50},
	number = {90},
	year = {2014},
	month = {OCT},
	pages = {13874-13884},
	publisher = {ROYAL SOC CHEMISTRY},
	address = {THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND},
	abstract = {<p>Structural mimicry of peptides has witnessed perceptible progress in the last three decades. Reverse turn and beta-hairpin units are the smallest secondary structural motifs that are some of the most scrutinized functional cores of peptides and proteins. The practice of mimicking, without altering the function of the bioactive core, ranges from conformational locking of the basic skeleton to total replacement of structural architecture using synthetic analogues. Development of heterogeneous backbones - using unnatural residues in place of natural ones - has broadened further opportunities for efficient structural rigidification. This feature article endeavours to trail the path of progress achieved hitherto and envisage the possibilities that lie ahead in the development of synthetic turn mimetics and hairpin nucleators.</p>},
	issn = {1359-7345},
	doi = {10.1039/c4cc03114h},
	author = {Nair, Roshna V. and Baravkar, Sachin B. and Ingole, Tukaram S. and Sanjayan, Gangadhar J.}
}
