Conformational heterogeneity of tripeptides containing Boc-Leu-Aib as corner residues in the solid stateHaldar, D., Drew, M.G.B. and Banerjee, A. (2007) Conformational heterogeneity of tripeptides containing Boc-Leu-Aib as corner residues in the solid state. Tetrahedron, 63 (25). pp. 5561-5566. ISSN 0040-4020 Full text not archived in this repository. It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1016/j.tet.2007.04.026 Abstract/SummaryA critical analysis of single crystal X-ray diffraction studies on a series of terminally protected tripeptides containing a centrally positioned Aib (alpha-aminoisobutyric acid) residue has been reported. For the tripeptide series containing Boc-Ala-Aib as corner residues, all the reported peptides formed distorted type II beta-turn structures. Moreover, a series of Phe substituted analogues ( tripeptides with Boc-Phe-Aib) have also shown different beta-turn conformations. However, the Leu-modified analogues (tripeptides with Boc-Leu-Aib) disrupt the concept of beta-turn formation and adopt various conformations in the solid state. X-ray crystallography sheds some light on the conformational heterogeneity at atomic resolution. (c) 2007 Elsevier Ltd. All rights reserved.
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