Conformational analysis by HRMAS NMR spectroscopy of resin-bound homo-peptides from Cα-methyl-leucine

Mario Rainaldi; Nathalie Lancelot; Karim Elbayed; Jesus Raya; Martial Piotto; Jean-Paul Briand; Bernard Kaptein; Quirinus B. Broxterman; Albrecht Berkessel; Fernando Formaggio; Claudio Toniolo; Alberto Bianco

doi:10.1039/B303193D

Conformational analysis by HRMAS NMR spectroscopy of resin-bound homo-peptides from C^α-methyl-leucine

Mario Rainaldi,^a Nathalie Lancelot,^b Karim Elbayed,^b Jesus Raya,^b Martial Piotto,^c Jean-Paul Briand,^d Bernard Kaptein,^e Quirinus B. Broxterman,^e Albrecht Berkessel,^f Fernando Formaggio,^a Claudio Toniolo^a and Alberto Bianco*^d

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* Corresponding authors

^a Institute of Biomolecular Chemistry, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italy

^b Institute of Chemistry, FRE 2446 CNRS-Bruker, Louis Pasteur University, 67084 Strasbourg, France

^c FRE 2446 CNRS-Bruker, 67160 Wissembourg, France

^d Institute of Molecular and Cellular Biology, UPR 9021 CNRS, 67084 Strasbourg, France
E-mail: A.Bianco@ibmc.u-strasbg.fr
Fax: +33 388 610680
Tel: +33 388 417088

^e DSM Research, Life Sciences, Advanced Synthesis and Catalysis, P. O. Box 18, 6160 MD Geleen, The Netherlands

^f Institute of Organic Chemistry, University of Köln, D-50939 Köln, Germany

Abstract

A series of [L-(αMe)Leu]_n (n = 1–5) homo-peptides have been covalently linked to Tentagel and POEPOP resins and submitted to a conformational study using HRMAS NMR spectroscopy. Whereas the mono- and dipeptide are mainly fully-extended, stable 3₁₀-helical structures are formed beginning from the trimer.

Organic & Biomolecular Chemistry

Conformational analysis by HRMAS NMR spectroscopy of resin-bound homo-peptides from C^α-methyl-leucine

Abstract

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Conformational analysis by HRMAS NMR spectroscopy of resin-bound homo-peptides from C^α-methyl-leucine

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