@article { ISI:000241179400014,
	title = {Hybrid foldamer with unique architecture from conformationally constrained aliphatic-aromatic amino acid conjugate},
	journal = {Tetrahedron},
	volume = {62},
	number = {43},
	year = {2006},
	month = {OCT},
	pages = {10141-10146},
	publisher = {PERGAMON-ELSEVIER SCIENCE LTD},
	type = {Article},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND},
	abstract = {<p>In this paper, we describe the design and synthesis of a novel hybrid foldamer, derived from a conformationally constrained aliphatic-aromatic amino acid conjugate that adopts a well-defined, compact, three-dimensional structure, governed by a combined conformational restriction imposed by the individual amino acids from which the foldamer is composed. Conformational investigations confirmed the prevalence of a unique doubly bent conformation for the foldamer, in both solid and solution states, as evidenced from single crystal X-ray and 2D NOESY studies, respectively. The findings suggest that constrained aliphatic-aromatic amino acid conjugates offer new avenues for the de novo design of hybrid foldamers with distinctive structural architectures. Furthermore, the de novo design strategy disclosed herein has the potential for significantly augmenting the {\textquoteleft}tool-box{\textquoteright} of the modern day peptidominetic chemist, as well as providing a novel approach to the field of rational design. (c) 2006 Elsevier Ltd. All rights reserved.</p>},
	keywords = {Amino acids, Conformation, Foldamer, Peptidomimetics},
	issn = {0040-4020},
	doi = {10.1016/j.tet.2006.08.032},
	author = {Srinivas, Deekonda and Gonnade, Rajesh G. and Ravindranathan, Sapna and Sanjayan, Gangadhar J.}
}
@article { ISI:000304570000010,
	title = {Expanding the structural repertoire of beta/alpha Ant-Pro (anthranilic acid-proline) oligomers into gamma/alpha 2-Amb-Pro (2-aminomethyl benzoic acid-proline) oligomers},
	journal = {Tetrahedron},
	volume = {68},
	number = {23},
	year = {2012},
	month = {JUN},
	pages = {4399-4405},
	publisher = {PERGAMON-ELSEVIER SCIENCE LTD},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND},
	abstract = {<p>In this article, we report a novel class of heterogeneous synthetic oligomers featuring the conformationally constrained amino acid residues - 2-aminomethyl benzoic acid (2-Amb) and proline (Pro) in repeating sequences. Oligomers as large as hexadecamers featuring the conformationally restricted gamma/alpha 2-Amb-Pro motif have been assembled using solution-phase Boc strategy, following multi-step synthetic sequences starting from the commercially available O-toluic acid. EDC-mediated peptide coupling has been found to be optimum for the assembly of the relatively non-polar oligomers, which could be readily purified by the standard column chromatographic purification procedures. This study offers considerable prospects of expanding the structural repertoire of beta/alpha Ant-Pro motif, which has been described earlier to assume right-handed helical architecture displaying robust nine-membered-ring closed network of hydrogen-bonding interactions, into gamma/alpha 2-Amb-Pro motif. (C) 2012 Elsevier Ltd. All rights reserved.</p>},
	keywords = {Amino acids, Foldamer, Peptides, Proline, Synthetic oligomers},
	issn = {0040-4020},
	doi = {10.1016/j.tet.2012.02.006},
	author = {Ramesh, Veera V. E. and Priya, Gowri and Rajamohanan, P. R. and Hofmann, Hans-Joerg and Sanjayan, Gangadhar J.}
}
