@article { ISI:000293230300022,
	title = {Concurrent display of both alpha- and beta-turns in a model peptide},
	journal = {Organic \& Biomolecular Chemistry},
	volume = {9},
	number = {16},
	year = {2011},
	month = {MAY},
	pages = {5762-5765},
	publisher = {ROYAL SOC CHEMISTRY},
	address = {THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND},
	abstract = {<p>This article describes a model peptide that concurrently displays both alpha- and beta-turns, as demonstrated by structural investigations using single crystal X-ray crystallography and solution-state NMR studies. The motif reported herein has the potential for the design of novel conformationally ordered synthetic oligomers with structural architectures distinct from those classically observed.</p>},
	issn = {1477-0520},
	doi = {10.1039/c1ob05553d},
	author = {Srinivas, Deekonda and Vijayadas, Kuruppanthara N. and Gonnade, Rajesh G. and Phalgune, Usha D. and Rajamohanan, Pattuparambil R. and Sanjayan, Gangadhar J.}
}
@article { ISI:000349401300020,
	title = {Conformational modulation of peptides using beta-amino benzenesulfonic acid ((S)Ant)},
	journal = {Organic \& Biomolecular Chemistry},
	volume = {13},
	number = {7},
	year = {2015},
	month = {DEC},
	pages = {2087-2091},
	publisher = {ROYAL SOC CHEMISTRY},
	address = {THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND},
	abstract = {<p>This communication describes the utility of a conformationally restricted aromatic beta-amino acid (2-aminobenzenesulfonic acid, (S)Ant) inducing various folding interactions in short peptides. Sandwiching (S)Ant between diverse amino acid residues was shown to form robust folded architectures featuring a variety of H-bonded networks, suggesting its utility in inducing peptide folding.</p>},
	issn = {1477-0520},
	doi = {10.1039/c4ob02421d},
	author = {Priya, Gowri and Kotmale, Amol S. and Chakravarty, Debamitra K. and Puranik, Vedavati G. and Rajamohanan, Pattuparambil R. and Sanjayan, Gangadhar J.}
}
@article {44153,
	title = {Cucurbit[7]uril induced formation of fret-enabled unilamellar lipid vesicles},
	journal = {Langmuir},
	volume = {33},
	year = {2017},
	month = {OCT},
	pages = {10989-10999},
	type = {Article},
	abstract = {A unique fluorescence resonance energy transfer (FRET) process is found to be operational in a unilamellar lipid self-assembly in the aqueous phase. A newly synthesized naphthyl based long chain lipid derivative [N-(naphthalene-1-ylmethyl)tetradecane-1-ammonium chloride, 14NA(+)] forms various self-assembled architectures in the aqueous phase. Controlled changes in lipid concentration lead to a transition of the self-assemblies from micelles to vesicles to rods. In the presence of cucurbit[7]uril (CB7), 14NA(+) forms a host-guest [2]pseudorotaxane complex (CB7(sic)14NA(+)) and secondary interactions lead to the formation of a lipid bilayer with hydrophobic pockets situated in between the layers. The change in the structure of 14NA(+) assemblies, interaction with CB7 and formation of supramolecular assemblies of CB7(sic)14NA(+) were examined using light scattering, spectroscopic, and microscopic techniques. Entrapment of a luminescent dye, anthracene within the hydrophobic bilayer of the supramolecular assembly CB7(sic)14NA(+) favors a modified luminescent response due to an efficient FRET process. Further, the FRET process could be controlled by thermal and chemical stimuli that induce transformation of unilamellar vesicles.},
	doi = {10.1021/acs.langmuir.7b02777},
	author = {Kushwaha, Shilpi and Maity, Arunava and Gangopadhyay, Monalisa and Ravindranathan, Sapna and Rajamohanan, Pattuparambil R. and Das, Amitava}
}
@article {44438,
	title = {Conformational studies of Ant-Pro motif-incorporated cyclic peptides: gramicidin S and avellanin},
	journal = {New Journal of Chemistry},
	volume = {42},
	year = {2018},
	month = {JAN},
	pages = {1197-1201},
	abstract = {This paper reports conformational changes observed in cyclic bioactive peptides such as gramicidin S and avellanin upon incorporation of a pseudo-beta (C9) Ant-(D)Pro turn motif in their structural frameworks. Solution-state studies suggested that a synthetic gramicidin S analog exhibits a beta-sheet conformation with C9 and C17 intramolecular hydrogen bonding patterns, while its truncated analog disturbs the beta-sheet conformation. Structural details were obtained using a combination of CD studies, X-ray crystal structure studies and nOe-based MD simulation studies.},
	doi = {10.1039/c7nj03701e},
	author = {Kotmale, Amol S. and Sangtani, Ekta and Gonnade, Rajesh G. and Sarkar, Dhiman and Burade, Sachin and Rajamohanan, Pattuparambil R. and Sanjayan, Gangadhar J.}
}
