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<p>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.</p>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-001502nas a2200181   4500008004100000022001400041245014500055210006900200260010600269300001400375490000700389520070700396100002301103700002401126700002401150700002801174856011801202       2008                        eng d  a0040-403900aPre-organization-mediated macrocylization: efficient synthesis and structural investigations of BINOL-m-phenylenediamine-derived macrocycles0 aPreorganizationmediated macrocylization efficient synthesis and   aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcMAR  a2139-21420 v493 a<p>This letter describes a serendipitous discovery of an efficient synthetic route to BINOL-m-phenylenediamine-derived macrocycles. These macrocycles are quickly accessible in an one-pot procedure by the direct condensation of (R) and (S) BINOL bis-acids with suitably substituted m-phenylenediamine analogs. Structural investigations by single crystal X-ray crystallography and solution-state NMR studies provided convincing evidence of their intramolecular hydrogen bonding arrangement and rigid structural architecture. The striking feature of these macrocycles is their ready accessibility in optically pure form coupled with their ease of synthesis. (C) 2008 Elsevier Ltd. All rights reserved.</p>1 aSrinivas, Deekonda1 aGonnade, Rajesh, G.1 aRajamohanan, P., R.1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/pre-organization-mediated-macrocylization-efficient-synthesis-and-structural-001208nas a2200205   4500008004100000022001400041245007200055210006900127260011000196300001400306490000600320520041000326100002300736700003300759700002400792700002300816700003500839700002800874856010000902       2011                        eng d  a1477-052000aConcurrent display of both alpha- and beta-turns in a model peptide0 aConcurrent display of both alpha and betaturns in a model peptid  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcMAY  a5762-57650 v93 a<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>1 aSrinivas, Deekonda1 aVijayadas, Kuruppanthara, N.1 aGonnade, Rajesh, G.1 aPhalgune, Usha, D.1 aRajamohanan, Pattuparambil, R.1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/concurrent-display-both-alpha-and-beta-turns-model-peptide-0