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-0