01946nas a2200229 4500008004100000022001400041245011900055210006900174260010600243300001600349490000700365520104600372653001601418653001701434653001301451653002001464100002301484700002401507700002601531700002801557856013101585 2006 eng d a0040-402000aHybrid foldamer with unique architecture from conformationally constrained aliphatic-aromatic amino acid conjugate0 aHybrid foldamer with unique architecture from conformationally c aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcOCT a10141-101460 v623 a

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.

10aAmino acids10aConformation10aFoldamer10aPeptidomimetics1 aSrinivas, Deekonda1 aGonnade, Rajesh, G.1 aRavindranathan, Sapna1 aSanjayan, Gangadhar, J. uhttps://library.ncl.res.in/content/hybrid-foldamer-unique-architecture-conformationally-constrained-aliphatic-aromatic-amino-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

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.

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-002051nas a2200253 4500008004100000022001400041245011600055210006900171260007700240300001400317490000700331520111700338653001601455653002601471653001401497653002101511653001301532653002601545100002101571700003301592700001401625700002801639856013001667 2014 eng d a1434-193X00aHeterogeneous foldamers from aliphatic-aromatic amino acid building blocks: current trends and future prospects0 aHeterogeneous foldamers from aliphaticaromatic amino acid buildi aBOSCHSTRASSE 12, D-69469 WEINHEIM, GERMANYbWILEY-V C H VERLAG GMBHcDEC a7763-77800 v463 a

Chemists' constant pursuit of understanding of the underlying principles of nature's most intricate phenomenon such as protein folding has led to the development of the field of foldamers. The emergence of diverse classes of unnatural amino acid building blocks has unleashed countless opportunities to design, develop and explore the structural and functional aspects of synthetic peptides. One current trend in foldamer chemistry is the heterofoldamer approach, which involves systematic stoichiometric variation of various natural/unnatural amino acid residues, leading to conformational ordering with intriguing structural architectures. In this regard, the incorporation of aromatic amino acids provides efficient structural rigidification and tunability to the molecular scaffolds, which can exhibit a range of secondary structural features. Recent times have witnessed an upsurge of foldamers featuring aliphatic-aromatic residues with diverse structural propensities. This review is an effort to cover this rapidly developing field of foldamer science and also to envisage its future perspectives.

10aAmino acids10aConformation analysis10aFoldamers10ahydrogen bonding10aPeptides10aStacking interactions1 aNair, Roshna, V.1 aVijayadas, Kuruppanthara, N.1 aRoy, Arup1 aSanjayan, Gangadhar, J. uhttps://library.ncl.res.in/content/heterogeneous-foldamers-aliphatic-aromatic-amino-acid-building-blocks-current-trends-and-0