HRMAS-NMR monitoring of the assembly of resin-bound aggregating sequences:effect of the peptide loading and the sovlent system

摘要

Despite all the continuous effort to optimize the peptide synthesis protocol,serious shortcomings have intriguingly persisted.They are mainly related to incomplete coupling during peptide growth casued by chain aggregation inside the bead [1].In addition,attempts to establish the results that grown resin solvation have been the object of several studies,as this propety has been found to depend upon the resin,peptide sequence,temperature and loading,as well as the solvent system [2,3,4].In this context,the use of spectroscopic methods in solid phase peptide synthesis can provide direct information regarding the conformationa features of peptide chains inside the polymer matrix.For this purpose a great variety of spectroscopic techniques,such as CD,FTIR,EPR and more recently the high-resolution magic angle spinning HRMAS NMR [5,6] spectroscopy,have been used.In the present work,we describe the use of (HRMAS) NMR specroscopy for monitoring the influence of the number of peptides chains and length of sequence on the solvation property of resin [7].