𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Conformational structure of the MOG-derived peptide 101–108 in solution

✍ Scribed by Carlo Guardiani; Simone Marsili; Stefania Marchetti; Cecilia Gambi; Piero Procacci; Roberto Livi

Publisher
Wiley (John Wiley & Sons)
Year
2011
Tongue
English
Weight
315 KB
Volume
96
Category
Article
ISSN
0006-3525

No coin nor oath required. For personal study only.

✦ Synopsis

One of the most important targets in the autoimmune attack in experimental autoimmune encephalomyielitis is the myelin oligodendrocyte glycoprotein (MOG). The complex with demyelinating 8-18C5 antibody was recently resolved by X-ray crystallography, showing a remarkable adhesion of the 101-108 MOG subsequence to the heavy chain of the autoantibody. In this study, we have determined, using replica exchange molecular dynamics methods, the structure of the MOG-derived peptide 101-108 in solution at ambient conditions. According to the simulation, the peptide exhibits, with significant probability, a distorted beta-turn structure highly similar to that of the corresponding subsequence in the crystal in complex with 8-18C5 antibody. Such results are found to be fully consistent with circular dichroism spectra of the peptide in solution, suggesting the use of the MOG-derived 101-108 peptide as a potential lead compound for designing decoy targets for the autoimmune attack in multiple sclerosis.

📜 SIMILAR VOLUMES

The conformational preferences of γ-lact
The conformational preferences of γ-lactam and its role in constraining peptide structure
✍ P. K. C. Paul; P. A. Burney; M. M. Campbell; D. J. Osguthorpe 📂 Article 📅 1990 🏛 Springer Netherlands 🌐 English ⚖ 849 KB

The conformational constraints imposed by 7-1actams in peptides have been studied using valence force field energy calculations and flexible geometry maps. It has been found that while cyclisation restrains the ~u of the lactam, non-bonded interactions contribute to the constraints on ~0 of the lact