Tri(propylene glycol) glycerolate diacrylate cross‐linked polystyrene: a new resin support for solid‐phase peptide synthesis

Abstract

A highly flexible, mechanically and chemically stable copolymer, tri(propylene glycol) glycerolate diacrylate cross-linked polystyrene (PS-TRPGGDA), was synthesized by the suspension polymerization and employed as a solid support for peptide synthesis. The beaded polymer support containing secondary hydroxyl functional groups in the cross-linker was used as the growth site for peptide synthesis. The procedure is unique and cost-effective in that it avoids the initial functionalization steps required for most of the styrene-based polymer supports. The resin was characterized by 13C-CP-MAS NMR spectroscopy and the morphologic features of the resin were investigated using scanning electron microscopy. Swelling studies conducted on the new support revealed that the PS-TRPGGDA resin undergoes more effective swelling and solvation than PS-DVB resin in all solvents used in peptide synthesis. The efficiency of the new support was demonstrated by synthesizing a 'difficult' sequence Ala-Arg-(Ala)6-Lys and comparing it with commercially available Merrifield and Sheppard resins. The synthetic efficiency was further demonstrated by the synthesis of a 24-residue NR 2A peptide substrate of calcium/calmodulin-binding peptide. The high yield and purity of the peptide synthesized on the novel support indicates the positive role of the flexible and hydrophilic cross-linking agent in the solid support.

The synergy of ChemMatrix resin® and pseudoproline building blocks renders Rantes, a complex aggregated chemokine

“…Although the synthesis of peptides containing hindered amino acids can be accomplished by the concourse of highly reactive coupling methods10, 11 such as HATU 12 or N,N,N ′, N ′‐tetramethylformamidinium hexafluorophosphate (TFFH),13 that of large and well‐structured peptides requires additional synthetic tools. In such cases, intra‐ and interchain interactions can be minimized by special solvents, such as the so‐called magic mixtures14 or those containing chaotropic salts,15 by structure disrupters such as Pro residues16 or protected amide bonds,17 and by resins that facilitate the solvation of peptide chains 18, 19…”

Study of the effect of the peptide loading and solvent system in SPPS by HRMAS-NMR

“…In this respect, solid phase peptide synthesis (SPPS) [3] has also continuously been selected as a target methodology for spectroscopic investigations, including CD [4], FTIR [5][6][7] and EPR [8][9][10][11][12]. In addition, NMR spectroscopy has been employed in this area [13][14][15] with emphasis on the high-resolution magic angle spinning (HRMAS-NMR) [16][17][18][19] technique applicable to the broad field of solid phase organic synthesis. The ability of this versatile spectroscopy has been valuable to obtain high quality NMR data on resin bound molecules including peptides [20][21][22][23][24][25] or even to compare the structural features of different polymeric materials [21,22,26].…”