Influence of amino acid and N-terminal protection residue structures on peptide p-nitroanilide adsorption on polystyrene-based support

被引:0
|
作者
Kolesnichenko, Alena V. [1 ]
Kazmina, Nathalia A. [1 ]
Chistov, Alexey A. [1 ]
Vakhrenev, Roman G. [1 ]
Kolesanova, Ekaterina F. [1 ]
机构
[1] Inst Biomed Chem, 10-8 Pogodinskaya Ul, Moscow 119121, Russia
关键词
Peptide-p-nitroanilides; Oxone(& REG; Desalting; Bio-Beads(& REG; ) SM-2; Adsorption chromatography; Phenyl group; SOLID-PHASE SYNTHESIS; PROTEASE; STRATEGY; REMOVAL; ASSAY;
D O I
10.1007/s00726-023-03302-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Polystyrene-based support Bio-Beads((R)) SM-2 was employed for desalting peptide-p-nitroanilides from Oxone((R)). Neither tosyl, 9-fluorenyl(methoxycarbonyl), p-nitroanilide groups nor indolyl or p-hydroxyphenyl side-chains of Trp and Tyr ensured an efficient adsorption of peptide-p-nitroanilides onto Bio-Beads((R)) SM-2. Only unsubstituted phenyl-containing protection groups (carbobenzoxy or benzoyl) and Phe residues provided the adsorption of peptides on Bio-Beads((R)) SM-2 and their efficient desalting. This support is well suitable for multiple parallel phenyl group-containing peptide derivative separations and high-throughput screenings.
引用
收藏
页码:1137 / 1140
页数:4
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