@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.}
}
@article {43996,
	title = {Structural insights into the hydrogen-bonding and folding pattern in ant-ant-pro-gly tetrapeptides},
	journal = {European Journal of Organic Chemistry},
	year = {2017},
	month = {MAY},
	pages = {2944{\textendash}2949},
	type = {Article},
	abstract = {In this paper, we provide structural insights into the hydrogen-bonding and folding pattern in Ant-Ant-Pro-Gly tetrapeptides (Ant: anthranilic acid; Pro: proline; and Gly: glycine). Comparison of the C-terminal esters and their amide analogs revealed strikingly different H-bonding networks. Whereas the ester analogs displayed an open structure without terminal H-bonding interactions, the amide analogs showed a completely folded structure. Structural details were revealed by using a combination of X-ray crystal structure studies and NOE-based molecular dynamics (MD) simulation studies.},
	doi = {10.1002/ejoc.201700181},
	author = {Baravkar, Sachin B. and Kotmale, Amol S. and Mobin, Samir R. and Gonnade, Rajesh Ghanshyam and Sanjayan, Gangadhar J.}
}
@article {45366,
	title = {Synthesis and anticancer activity of conformationally constrained Smac mimetics containing pseudo beta turns},
	journal = {Tetrahedron Letters },
	volume = {59},
	year = {2018},
	month = {SEP},
	pages = {3473-3476},
	type = {Article},
	abstract = {Herein, we report synthesis and in vitro anticancer activity of conformationally constrained Smac mimetics containing reverse turn inducing motifs "Ant-Pro" and "sAnt-Pro". The synthesis of Smac analogs with diverse hydrophobic groups at the C-terminus was carried out using solution phase peptide synthesis. The synthesis of Ant-Pro containing analogs 3a-j was carried out by ring opening of benzoxazinones 7a-c, whereas, their sulfonamide counterparts 4a-h were synthesized by using routine acid-amine coupling reaction. In vitro anticancer studies against breast cancer cell line MDA-MB-231 revealed that some of the new analogs had better anticancer activity than the standard AVPI Smac tetrapeptide. (C) 2018 Published by Elsevier Ltd.},
	doi = {10.1016/j.tetlet.2018.08.016},
	author = {Baravkar, Sachin B. and Wagh, Mahendra A. and Paul, Debasish and Santra, Manas and Sanjayan, Gangadhar J.}
}
