Syntheses, characterization and application of crosslinked polystyrene-ethyleneglycol acrylate resin (CLPSER) as a novel polymer support for polypeptide syntheses
S. Leena et Ks. Kumar, Syntheses, characterization and application of crosslinked polystyrene-ethyleneglycol acrylate resin (CLPSER) as a novel polymer support for polypeptide syntheses, J PEPT RES, 58(2), 2001, pp. 117-128
Cross-linked polystyrene-ethyleneglycol acrylate resin (CLPSER) was develop
ed for the solid-phase synthesis of peptide by introducing a cross-linker O
,O'- bis(2-acrylamidopropyl)polyethylene glycol(1900) (Acr(2)PEG), into pol
ystyrene. The cross-linker was prepared by treating acryloyl chloride with
O,O'-bis(2-aminopropyl) polyethylene glycol(1900) [(NH2)(2)PEG] in the pres
ence of diisopropylethylamine. The copolymer was prepared either by bulk or
inverse suspension copolymerization of Acr(2)PEG(1900) and styrene using s
orbitan monolaurate as the suspension stabilizer, and a mixture of ammonium
peroxodisulfate and benzoyl peroxide as the radical initiators. The resin
was characterized using gel-phase C-13 NMR, infrared (KBr) spectroscopic te
chniques and the morphological features of the resin were investigated usin
g scanning electron microscopy photographs. CLPSER showed excellent swellin
g in a broad range of solvents and was found to be chemically inert to vari
ous reagents and solvents used in solid-phase peptide synthesis. To demonst
rate the usefulness of the new resin in polypeptide synthesis, the support
was derivatized with an 'internal reference' amino acid (norleucine) and a
handle 4-(4-hydroxymethyl-3-methoxy)butyric acid. The new resin was compare
d with commercial supports such as Merrifield and Sheppard resins by synthe
sizing an acyl carrier protein (65-74) fragment under the same experimental
conditions. HPLC profiles revealed the high efficiency of the newly develo
ped support. Resin capability in peptide synthesis was further demonstrated
by the solid phase synthesis of a 25-residue peptide from the E2/NS1 regio
n hepatitis C viral polyprotein.