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The polypeptide 310-helix as a template and a spacer |
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| Authors: | Marco Crisma Alberto Bianco Fernando Formaggio Claudio Toniolo Johan Kamphuis |
| Affiliation: | (1) Biopolymer Research Centre, C.N.R., Department of Organic Chemistry, University of Padova, Via Marzolo 1, I-35131 Padova, Italy;(2) Bioorganic Chemistry Section, DSM Research, 6160 MD Gellen, The Netherlands |
| Abstract: | Summary X-ray diffraction analyses have provided detailed structural information on the 310-helices of (i) pBrBz-d-( Me)Phe-(Aib)2-d-(Me)Phe-Aib-OtBu and Ac-(Aib)2-l-Lys(Bz)-(Aib)2-l-Lys(Bz)-(Aib)2-NHMe as suitable templates for molecular recognition studies, and (ii) pBrBz-TOAC-(l-Ala)2-TOAC-l-Ala-NHtBu as an appropriate spacer for an ESR study of side chain to side chain interactions. In addition, in Ac-TOAC-(Aib)2-l-Trp-Aib-OMe, forming a 310-helix, the TOAC residue plays the role of an effective quencher of the fluorescence of the tryptophan residue located one turn apart. |
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