@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 {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.}
}
