01587nas a2200277   4500008004100000022001400041245012600055210006900181260007700250300001200327490000700339520055600346653001600902653002500918653001700943653003000960653001800990100002401008700002101032700002401053700002601077700002401103700002401127700002801151856013001179       2007                        eng d  a0935-964800aEnforcing periodic secondary structures in hybrid peptides: a novel hybrid foldamer containing periodic gamma-turn motifs0 aEnforcing periodic secondary structures in hybrid peptides a nov  aPO BOX 10 11 61, D-69451 WEINHEIM, GERMANYbWILEY-V C H VERLAG GMBHcJAN  a636-6390 v723 a<p>{This note describes the design, synthesis, and conformational studies of a novel hybrid foldamer that adopts a definite compact, three-dimensional structure determined by a combined effect of the special conformational properties of the foldamer constituents. The striking feature of this de novo designed foldamer is its ability to display periodic gamma-turn conformations stabilized by intramolecular hydrogen bonds. Conformational investigations by single-crystal X-ray studies, solution-state NMR, and ab initio MO theory at the HF/6-31G*</p>10aammonia-TPD10abenzylation reaction10aCe-Al-MCM-4110aFriedel-Crafts alkylation10apyridine-FrIR1 aBaruah, Pranjal, K.1 aSreedevi, N., K.1 aGonnade, Rajesh, G.1 aRavindranathan, Sapna1 aDamodaran, Krishnan1 aHofmann, Hans-Joerg1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/enforcing-periodic-secondary-structures-hybrid-peptides-novel-hybrid-foldamer-containing-001017nas a2200181   4500008004100000022001400041245008800055210006900143260011000212300001400322520025200336100002300588700002400611700003500635700002400670700002800694856011300722       2008                        eng d  a1359-734500aFoldamers with unusual structural architecture from spirobi(indane) building blocks0 aFoldamers with unusual structural architecture from spirobiindan  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcJUN  a2541-25433 a<p>This communication demonstrates the utility of inherently rigid building blocks such as 1,1'-spirobi(indane) for generating conformationally ordered synthetic oligomers with structural architectures distinct from those classically observed.</p>1 aKendhale, Amol, M.1 aGonnade, Rajesh, G.1 aRajamohanan, Pattuparambil, R.1 aHofmann, Hans-Joerg1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/foldamers-unusual-structural-architecture-spirobiindane-building-blocks-002283nas a2200229   4500008004100000022001400041245008800055210006900143260007100212300001600283490000800299520143600307100002601743700002201769700002601791700002401817700001801841700002601859700002401885700002801909856011601937       2008                        eng d  a0002-786300aSequence-specific unusual (1 -> 2)-type helical turns in alpha/beta-hybrid peptides0 aSequencespecific unusual 1 2type helical turns in alphabetahybri  a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcDEC  a17743-177540 v1303 a<p>This article describes novel conformationally ordered (alpha/beta-hybrid peptides consisting of repeating L-proline-anthranilic acid building blocks. These oligomers adopt a compact, right-handed helical architecture determined by the intrinsic conformational preferences of the individual amino acid residues. The striking feature of these oligomers is their ability to display an unusual periodic pseudo beta-turn network of nine-membered hydrogen-bonded rings formed in the forward direction of the sequence by 1–&gt;2 amino acid interactions both in solid-state and in solution. Conformational investigations of several of these oligomers by single-crystal X-ray diffraction, solution-state NMR, and ab initio MO theory suggest that the characteristic steric and dihedral angle restraints exerted by proline are essential for stabilizing the unusual pseudo beta-turn network found in these oligomers. Replacing proline by the conformationally flexible analogue alanine (Ala) or by the conformationally more constrained alpha-amino isobutyric acid (Aib) had an adverse effect on the stabilization of this structural architecture. These findings increase the potential to design novel secondary structure elements profiting from the steric and dihedral angle constraints of the amino acid constituents and help to augment the conformational space available for synthetic oligomer design with diverse backbone structures.</p>1 aPrabhakaran, Panchami1 aKale, Sangram, S.1 aPuranik, Vedavati, G.1 aRajamohanan, P., R.1 aChetina, Olga1 aHoward, Judith, A. K.1 aHofmann, Hans-Joerg1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/sequence-specific-unusual-1-2-type-helical-turns-alphabeta-hybrid-peptides-001046nas a2200193   4500008004100000022001400041245008200055210006900137260011000206300001400316520024600330100002600576700002600602700002300628700003500651700002400686700002800710856011400738       2009                        eng d  a1359-734500aNovel foldamer structural architecture from cofacial aromatic building blocks0 aNovel foldamer structural architecture from cofacial aromatic bu  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcMAY  a3446-34483 a<p>This communication demonstrates the utility of peri-substituted 1,8-diphenylnaphthalene as an effective building block for the construction of novel conformationally ordered synthetic oligomers displaying cofacial structural features.</p>1 aPrabhakaran, Panchami1 aPuranik, Vedavati, G.1 aChandran, Jima, N.1 aRajamohanan, Pattuparampil, R.1 aHofmann, Hans-Joerg1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/novel-foldamer-structural-architecture-cofacial-aromatic-building-blocks-001183nas a2200205   4500008004100000022001400041245009100055210006900146260011000215300001400325490000600339520035800345100002600703700002600729700002300755700002400778700002400802700002800826856012300854       2009                        eng d  a1477-052000aSterically controlled naphthalene homo-oligoamides with novel structural architectures0 aSterically controlled naphthalene homooligoamides with novel str  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcMAR  a2458-24650 v73 a<p>Herein we report novel naphthalene homo-oligoamides, derived from 4-amino-3-methoxy-naphthalene-2-carboxylic acid and 4-amino-1-methoxy-naphthalene-2-carboxylic acid as monomer building blocks, that display an anti-periplanar arrangement of the naphthyl rings, primarily induced by steric interactions between adjacent groups and functionalities.</p>1 aPrabhakaran, Panchami1 aPuranik, Vedavati, G.1 aChandran, Jima, N.1 aRajamohanan, P., R.1 aHofmann, Hans-Joerg1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/sterically-controlled-naphthalene-homo-oligoamides-novel-structural-architectures-002049nas a2200253   4500008004100000022001400041245017300055210006900228260010600297300001400403490000700417520104900424653001601473653001301489653001301502653001201515653002401527100002501551700001701576700002401593700002401617700002801641856012601669       2012                        eng d  a0040-402000aExpanding the structural repertoire of beta/alpha Ant-Pro (anthranilic acid-proline) oligomers into gamma/alpha 2-Amb-Pro (2-aminomethyl benzoic acid-proline) oligomers0 aExpanding the structural repertoire of betaalpha AntPro anthrani  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcJUN  a4399-44050 v683 a<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>10aAmino acids10aFoldamer10aPeptides10aProline10aSynthetic oligomers1 aRamesh, Veera, V. E.1 aPriya, Gowri1 aRajamohanan, P., R.1 aHofmann, Hans-Joerg1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/expanding-structural-repertoire-betaalpha-ant-pro-anthranilic-acid-proline-oligomers-0