Conformational analysis by HRMAS NMR spectroscopy of resin-bound homo-peptides from C(alpha)-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(alpha)-methyl-leucine

Org Biomol Chem. 2003 Jun 7;1(11):1835-7. doi: 10.1039/b303193d.

Authors

Mario Rainaldi¹, Nathalie Lancelot, Karim Elbayed, Jesus Raya, Martial Piotto, Jean-Paul Briand, Bernard Kaptein, Quirinus B Broxterman, Albrecht Berkessel, Fernando Formaggio, Claudio Toniolo, Alberto Bianco

Affiliation

¹ Institute of Biomolecular Chemistry, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italy.

PMID: 12945760
DOI: 10.1039/b303193d

Abstract

A series of [L-(alphaMe)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 3(10)-helical structures are formed beginning from the trimer.

MeSH terms

Leucine / analogs & derivatives*
Nuclear Magnetic Resonance, Biomolecular / methods*
Oligopeptides / chemistry*
Protein Structure, Secondary
Resins, Synthetic

Substances

Oligopeptides
Resins, Synthetic
Leucine