Abstract
In this study, we report that the insertion of a pseudoproline dipeptide for the solid-phase peptide synthesis of wild-type Phospholamban protein (WT-PLB) has two important advantages. First, it disrupts the formation of different secondary structures, which is responsible for poor couplings during the preparation of highly aggregated sequences. Second, it enhances the purities and solubility of crude products leading to easier HPLC purification.
Highlights
Phospholamban (PLB) is a hydrophobic 52-amino acid transmembrane protein that is involved in regulating the contraction and relaxation of heart muscle [1,2,3]
We report that the insertion of a pseudoproline dipeptide for the solid-phase peptide synthesis of wild-type Phospholamban protein (WT-PLB) has two important advantages
It disrupts the formation of different secondary structures, which is responsible for poor couplings during the preparation of highly aggregated sequences
Summary
Phospholamban (PLB) is a hydrophobic 52-amino acid transmembrane protein that is involved in regulating the contraction and relaxation of heart muscle [1,2,3]. The isolation and purification of large quantities of native PLB through molecular biology techniques has not yet been achieved due to difficulties encountered in the bacterial over expression of phospholamban cDNA [4,5]. PLB has been prepared by chemical synthesis using standard solidphase peptide synthesis and purification in organic solvents [6, 7]. This approach gives the opportunity to synthesize site-specific isotopically labeled peptides and proteins [8,9,10]. The biochemical and biophysical comparison of synthetic PLB and native PLB revealed that they are both similar in size and functionally identical [6,7]
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