<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Srinivas, Deekonda</style></author><author><style face="normal" font="default" size="100%">Gonnade, Rajesh G.</style></author><author><style face="normal" font="default" size="100%">Ravindranathan, Sapna</style></author><author><style face="normal" font="default" size="100%">Sanjayan, Gangadhar J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Hybrid foldamer with unique architecture from conformationally constrained aliphatic-aromatic amino acid conjugate</style></title><secondary-title><style face="normal" font="default" size="100%">Tetrahedron</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino acids</style></keyword><keyword><style  face="normal" font="default" size="100%">Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Foldamer</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptidomimetics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">OCT</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">43</style></number><publisher><style face="normal" font="default" size="100%">PERGAMON-ELSEVIER SCIENCE LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">62</style></volume><pages><style face="normal" font="default" size="100%">10141-10146</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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 `tool-box' 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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">43</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">2.645</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Edwards, Alison A.</style></author><author><style face="normal" font="default" size="100%">Sanjayan, Gangadharar J.</style></author><author><style face="normal" font="default" size="100%">Hachisu, Shuji</style></author><author><style face="normal" font="default" size="100%">Tranter, George E.</style></author><author><style face="normal" font="default" size="100%">Fleet, George W. J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Novel series of oligomers from 4-aminomethyl-tetrahydrofuran-2-carboxylates with 2,4-cis and 2,4-trans stereochemistry</style></title><secondary-title><style face="normal" font="default" size="100%">Tetrahedron</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Foldamers</style></keyword><keyword><style  face="normal" font="default" size="100%">gamma amino acids</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptidomimetics</style></keyword><keyword><style  face="normal" font="default" size="100%">sugar amino acids</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">AUG</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">33</style></number><publisher><style face="normal" font="default" size="100%">PERGAMON-ELSEVIER SCIENCE LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">62</style></volume><pages><style face="normal" font="default" size="100%">7718-7725</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Two tetrahydrofuran-based y-amino acids [2,4-cis and 2,4-trans] were subjected to iterative peptide-coupling procedures to afford dimeric, tetrameric and hexameric carbopeptoids in good yield. These homooligomers were prepared for secondary structural study-to ascertain the conformational preference inherent in the monomer units. The L-xylo oligomers were protected with triethylsilyl ethers to increase the range of solvents suitable for structural investigation. Initial secondary structure data indicate the presence of hydrogen-bonded conformations in the L-ribo series. (c) 2006 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">33</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">2.645</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Edwards, Alison A.</style></author><author><style face="normal" font="default" size="100%">Sanjayan, Gangadhar J.</style></author><author><style face="normal" font="default" size="100%">Hachisu, Shuji</style></author><author><style face="normal" font="default" size="100%">Soengas, Raquel</style></author><author><style face="normal" font="default" size="100%">Stewart, Alistair</style></author><author><style face="normal" font="default" size="100%">Tranter, George E.</style></author><author><style face="normal" font="default" size="100%">Fleet, George W. J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Synthesis of 4-aminomethyl-tetrahydrofuran-2-carboxylates with 2,4-cis and 2,4-trans relationships</style></title><secondary-title><style face="normal" font="default" size="100%">Tetrahedron</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">gamma amino acids</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptidomimetics</style></keyword><keyword><style  face="normal" font="default" size="100%">scaffolds</style></keyword><keyword><style  face="normal" font="default" size="100%">sugar amino acids</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">APR</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">17</style></number><publisher><style face="normal" font="default" size="100%">PERGAMON-ELSEVIER SCIENCE LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">62</style></volume><pages><style face="normal" font="default" size="100%">4110-4119</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Templated tetrahydrofuran-based gamma-azido esters were prepared with the C-2 and C-4 functionalities in cis and trans relative configurations. This was achieved by ring contraction of the suitably protected 2-O-triflates of pentono-1,5-lactones (D-ribose and L-arabinose) with subsequent introduction of the azide via the 4-O-triflate. Access to a corresponding beta-azido ester was achieved in good yield. Little elimination product was observed by introduction of the azide via the 3-O-triflate. These azido esters are scaffolds. which may be predisposed to adopt secondary structural motifs, for example. for use as peptidomimetics; they may also be utilised for the preparation of stereodiverse compound libraries. (c) 2006 Elsevier Ltd All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">17</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">2.645</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Thorat, Vijaykumar H.</style></author><author><style face="normal" font="default" size="100%">Ingole, Tukaram S.</style></author><author><style face="normal" font="default" size="100%">Vijayadas, Kuruppanthara N.</style></author><author><style face="normal" font="default" size="100%">Nair, Roshna V.</style></author><author><style face="normal" font="default" size="100%">Kale, Sangram S.</style></author><author><style face="normal" font="default" size="100%">Ramesh, Veera V. E.</style></author><author><style face="normal" font="default" size="100%">Davis, Hilda C.</style></author><author><style face="normal" font="default" size="100%">Prabhakaran, Panchami</style></author><author><style face="normal" font="default" size="100%">Gonnade, Rajesh G.</style></author><author><style face="normal" font="default" size="100%">Gawade, Rupesh L.</style></author><author><style face="normal" font="default" size="100%">Puranik, Vedavati G.</style></author><author><style face="normal" font="default" size="100%">Rajamohanan, Pattuparambil R.</style></author><author><style face="normal" font="default" size="100%">Sanjayan, Gangadhar J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Ant-pro reverse-turn motif. structural features and conformational characteristics</style></title><secondary-title><style face="normal" font="default" size="100%">European Journal of Organic Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Peptides</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptidomimetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein folding</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein structures</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">17, SI</style></number><publisher><style face="normal" font="default" size="100%">WILEY-V C H VERLAG GMBH</style></publisher><pub-location><style face="normal" font="default" size="100%">BOSCHSTRASSE 12, D-69469 WEINHEIM, GERMANY</style></pub-location><pages><style face="normal" font="default" size="100%">3529-3542</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;This article details the characteristic conformational features of the Ant-Pro reverse turn ? a folded pseudo -turn motif that displays a closed nine-membered-ring hydrogen-bonded network involving just two amino acid residues, namely anthranilic acid (Ant; a constrained -amino acid), and proline (Pro; a constrained -amino acid). The results from the extensive investigation of ten crystal structures and their NMR conformations in the solution state provide a clear idea about the conformational characteristics of the Ant-Pro reverse turn. The Ant and Pro residues, which form the turn segment, maintain a perfect antiperiplanar orientation throughout, leaving little possibility for the formation of the otherwise possible six-membered hydrogen-bonding that requires a coplanar disposition of the two amino acid residues, as clearly evident from investigation of several crystal structures. The closed hydrogen-bonded network observed in the Ant-Pro reverse turn motif, formed in the forward direction of the sequence (12 amino acid interactions) involving only two amino acid residues, is in stark contrast to the native -turns that involve four residues to form hydrogen-bonded network featuring backward 14 amino acid interactions. The readily available two-residue Ant-Pro motif raises the possibility of a practical utility, particularly in the application of rigidifying flexible peptide backbones by inserting the robust Ant-Pro reverse turn motifs into their backbone.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">17</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.154
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Patil, Kiran M.</style></author><author><style face="normal" font="default" size="100%">Naik, Rangeetha J.</style></author><author><style face="normal" font="default" size="100%">Vij, Manika</style></author><author><style face="normal" font="default" size="100%">Yadav, Amit K.</style></author><author><style face="normal" font="default" size="100%">Kumar, Vaijayanti A.</style></author><author><style face="normal" font="default" size="100%">Ganguli, Munia</style></author><author><style face="normal" font="default" size="100%">Fernandes, Moneesha</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Second generation, arginine-rich (R-X `-R)(4)-type cell-penetrating alpha-omega-alpha-peptides with constrained, chiral omega-amino acids (X `) for enhanced cargo delivery into cells</style></title><secondary-title><style face="normal" font="default" size="100%">Bioorganic &amp; Medicinal Chemistry Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">(R-X-R)-motif</style></keyword><keyword><style  face="normal" font="default" size="100%">alpha-omega-alpha-Peptide</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell-penetrating peptide</style></keyword><keyword><style  face="normal" font="default" size="100%">Constrained chiral amino acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptidomimetics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">SEP</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">17</style></number><publisher><style face="normal" font="default" size="100%">PERGAMON-ELSEVIER SCIENCE LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">24</style></volume><pages><style face="normal" font="default" size="100%">4198-4202</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The syntheses of novel N-aminoalkyl proline-derived spacers (X') in polycationic (R-X'-R)-motif cell-penetrating alpha-omega-alpha-peptides are described as improved molecular transporters and their structural features studied by CD. FACS analysis shows enhanced cellular uptake and confocal microscopy indicates predominantly cytoplasmic localization. The oligomers are efficient at transporting pDNA into cells. The chirality together with the hydrophobicity and flexibility derived from the spacer chain are found to have marked influence on the cell-penetrating and cargo delivery properties of the cell-penetrating peptides (CPPs). The peptides containing N-(3-aminopropyl)-D-proline spacers are found to be the best at cell penetration and cargo delivery in the present study. (C) 2014 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">17</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">1.19</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ingole, Tukaram S.</style></author><author><style face="normal" font="default" size="100%">Vijayadas, Kuruppanthara N.</style></author><author><style face="normal" font="default" size="100%">Chaitanya, K. N.</style></author><author><style face="normal" font="default" size="100%">Kotmale, Amol S.</style></author><author><style face="normal" font="default" size="100%">Gawade, Rupesh L.</style></author><author><style face="normal" font="default" size="100%">Gonnade, Rajesh G.</style></author><author><style face="normal" font="default" size="100%">Rajamohanan, P. R.</style></author><author><style face="normal" font="default" size="100%">Sanjayan, Gangadhar J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Disruption of native beta-turns: consequence of folding competition between native and orthanilic acid proline-based pseudo beta-turn</style></title><secondary-title><style face="normal" font="default" size="100%">European Journal of Organic Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Conformation analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">hydrogen bonds</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptidomimetics</style></keyword><keyword><style  face="normal" font="default" size="100%">structure elucidation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2016</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">7</style></number><publisher><style face="normal" font="default" size="100%">WILEY-V C H VERLAG GMBH</style></publisher><pub-location><style face="normal" font="default" size="100%">POSTFACH 101161, 69451 WEINHEIM, GERMANY</style></pub-location><pages><style face="normal" font="default" size="100%">1380-1388</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Five tetrapeptides comprising beta-turn-forming elements and a pseudo beta-turn (C9 H-bonding) based on an SAntPro (orthanilic acid - proline) motif were designed and synthesized. Their extensive conformational investigation by single-crystal X-ray crystallography, solution-state 2D NMR spectroscopic, and nOe-restrained MD simulation studies revealed the formation of C14 or C9 folding and disruption of the native beta-turn (C10 H-bonding) architecture. The striking difference between the psi(psi(2)) angle of ``i + 2'' residues of native beta-turn and designed peptides suggest that formation of the native beta-turn is not favored. The results suggest that other turn-forming motifs can dramatically modulate the stability of the native beta-turn structure.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">7</style></issue><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">3.068</style></custom4></record></records></xml>