@article { ISI:000345826600002,
	title = {Heterogeneous foldamers from aliphatic-aromatic amino acid building blocks: current trends and future prospects},
	journal = {European Journal of Organic Chemistry},
	volume = {46},
	number = {35},
	year = {2014},
	month = {DEC},
	pages = {7763-7780},
	publisher = {WILEY-V C H VERLAG GMBH},
	address = {BOSCHSTRASSE 12, D-69469 WEINHEIM, GERMANY},
	abstract = {<p>Chemists{\textquoteright} constant pursuit of understanding of the underlying principles of nature{\textquoteright}s most intricate phenomenon such as protein folding has led to the development of the field of foldamers. The emergence of diverse classes of unnatural amino acid building blocks has unleashed countless opportunities to design, develop and explore the structural and functional aspects of synthetic peptides. One current trend in foldamer chemistry is the heterofoldamer approach, which involves systematic stoichiometric variation of various natural/unnatural amino acid residues, leading to conformational ordering with intriguing structural architectures. In this regard, the incorporation of aromatic amino acids provides efficient structural rigidification and tunability to the molecular scaffolds, which can exhibit a range of secondary structural features. Recent times have witnessed an upsurge of foldamers featuring aliphatic-aromatic residues with diverse structural propensities. This review is an effort to cover this rapidly developing field of foldamer science and also to envisage its future perspectives.</p>},
	keywords = {Amino acids, Conformation analysis, Foldamers, hydrogen bonding, Peptides, Stacking interactions},
	issn = {1434-193X},
	doi = {10.1002/ejoc.201402877},
	author = {Nair, Roshna V. and Vijayadas, Kuruppanthara N. and Roy, Arup and Sanjayan, Gangadhar J.}
}
@article { ISI:000372848000021,
	title = {Disruption of native beta-turns: consequence of folding competition between native and orthanilic acid proline-based pseudo beta-turn},
	journal = {European Journal of Organic Chemistry},
	number = {7},
	year = {2016},
	month = {MAR},
	pages = {1380-1388},
	publisher = {WILEY-V C H VERLAG GMBH},
	address = {POSTFACH 101161, 69451 WEINHEIM, GERMANY},
	abstract = {<p>Five tetrapeptides comprising beta-turn-forming elements and a pseudo beta-turn (C9 H-bonding) based on an SAntPro (orthanilic acid - proline) motif were designed and synthesized. Their extensive conformational investigation by single-crystal X-ray crystallography, solution-state 2D NMR spectroscopic, and nOe-restrained MD simulation studies revealed the formation of C14 or C9 folding and disruption of the native beta-turn (C10 H-bonding) architecture. The striking difference between the psi(psi(2)) angle of {\textquoteleft}{\textquoteleft}i + 2{\textquoteright}{\textquoteright} residues of native beta-turn and designed peptides suggest that formation of the native beta-turn is not favored. The results suggest that other turn-forming motifs can dramatically modulate the stability of the native beta-turn structure.</p>},
	keywords = {Conformation analysis, hydrogen bonds, Peptidomimetics, structure elucidation},
	issn = {1434-193X},
	doi = {10.1002/ejoc.201501558},
	author = {Ingole, Tukaram S. and Vijayadas, Kuruppanthara N. and Chaitanya, K. N. and Kotmale, Amol S. and Gawade, Rupesh L. and Gonnade, Rajesh G. and Rajamohanan, P. R. and Sanjayan, Gangadhar J.}
}
