@article { ISI:000307300900016,
	title = {Helical folding in heterogeneous foldamers without inter-residual backbone hydrogen-bonding},
	journal = {Chemical Communications},
	volume = {48},
	number = {71},
	year = {2012},
	month = {JUL},
	pages = {8922-8924},
	publisher = {ROYAL SOC CHEMISTRY},
	address = {THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND},
	abstract = {<p>This communication describes a set of hybrid foldamers that do not feature inter-residual, but intra-residual backbone hydrogen-bonding, yet adopt a preferentially folded conformation displaying right-handed helical architecture. Conformational ordering is apparently due to the combined conformational restrictions imposed by the conformationally restricted individual amino acid residues with which the oligomers are made of.</p>},
	issn = {1359-7345},
	doi = {10.1039/c2cc33235c},
	author = {Priya, Gowri and Kotmale, Amol S. and Gawade, Rupesh L. and Mishra, Deepti and Pal, Sourav and Puranik, Vedavati G. and Rajamohanan, Pattuparambil R. and Sanjayan, Gangadhar J.}
}
@article {44492,
	title = {Helically structured peptide architecture engineered using dimedone as a rigid organic scaffold},
	journal = {ChemistrySelect},
	volume = {3},
	year = {2018},
	month = {MAR},
	pages = {2776-2780},
	abstract = {This communication reports the use of a rigid organic scaffold to attach two unsymmetrical peptide chains on a single carbon atom. The approach describes the step-by-step attachment of peptide chains to the rigid dimedone template (5,5-dimethyl-1,3-cyclohexanedione) - a molecular scaffold that directs orientation of the peptide helices in a well-defined arrangement via intra-molecular hydrogen bonding. The overall topology of the final molecules was studied using CD spectroscopy which suggested existence of helical architecture.},
	doi = {10.1002/slct.201702856},
	author = {Nadimpally, Krishna C. and Madica, Krishnaprasad and Kotmale, Amol S. and Gonnade, Rajesh G. and Sanjayan, Gangadhar J.}
}
