@article { ISI:000304387800025,
	title = {Efficient total synthesis of calothrixin B},
	journal = {Tetrahedron Letters},
	volume = {53},
	number = {23},
	year = {2012},
	month = {JUN},
	pages = {2894-2896},
	publisher = {PERGAMON-ELSEVIER SCIENCE LTD},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND},
	abstract = {<p>An efficient synthesis of calothrixin B (2) is demonstrated starting from 9H-carbazol-4-ol, having two one-pot reaction sequences as key steps. As a novel observation, DMF-methanol was shown to be a hydride donor for reduction of aldehyde to alcohol. Unexpectedly, nucleophilic substitution of benzyloxy by methoxy group was observed. (C) 2012 Elsevier Ltd. All rights reserved.</p>},
	keywords = {Calothrixin B, CAN, DMF-methanol, Hydride donor},
	issn = {0040-4039},
	doi = {10.1016/j.tetlet.2012.03.131},
	author = {Bhosale, Shrikar M. and Gawade, Rupesh L. and Puranik, Vedavati G. and Kusurkar, Radhika S.}
}
@article { ISI:000328182900006,
	title = {Ester vs. amide on folding: a case study with a 2-residue synthetic peptide},
	journal = {Organic \& Biomolecular Chemistry},
	volume = {11},
	number = {48},
	year = {2013},
	month = {DEC},
	pages = {8348-8356},
	publisher = {ROYAL SOC CHEMISTRY},
	address = {THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND},
	abstract = {<p>Although known for their inferiority as hydrogen-bonding acceptors when compared to amides, esters are often found at the C-terminus of peptides and synthetic oligomers (foldamers), presumably due to the synthetic readiness with which they are obtained using protected peptide coupling, deploying amino acid esters at the C-terminus. When the H-bonding interactions deviate from regularity at the termini, peptide chains tend to {\textquoteleft}{\textquoteleft}fray apart{\textquoteright}{\textquoteright}. However, the individual contributions of C-terminal esters in causing peptide chain end-fraying goes often unnoticed, particularly due to diverse competing effects emanating from large peptide chains. Herein, we describe a striking case of a comparison of the individual contributions of C-terminal ester vs. amide carbonyl as a H-bonding acceptor in the folding of a peptide. A simple two-residue peptide fold has been used as a testing case to demonstrate that amide carbonyl is far superior to ester carbonyl in promoting peptide folding, alienating end-fraying. This finding would have a bearing on the fundamental understanding of the individual contributions of stabilizing/destabilizing non-covalent interactions in peptide folding.</p>},
	issn = {1477-0520},
	doi = {10.1039/c3ob41967c},
	author = {Vijayadas, Kuruppanthara N. and Nair, Roshna V. and Gawade, Rupesh L. and Kotmale, Amol S. and Prabhakaran, Panchami and Gonnade, Rajesh G. and Puranik, Vedavati G. and Rajamohanan, Pattuparambil R. and Sanjayan, Gangadhar J.}
}
