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

Alena V Kolesnichenko; Nathalia A Kazmina; Alexey A Chistov; Roman G Vakhrenev; Ekaterina F Kolesanova

doi:10.1007/s00726-023-03302-4

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

Amino Acids. 2023 Sep;55(9):1137-1140. doi: 10.1007/s00726-023-03302-4. Epub 2023 Jul 14.

Authors

Alena V Kolesnichenko^#¹, Nathalia A Kazmina^#¹, Alexey A Chistov¹, Roman G Vakhrenev¹, Ekaterina F Kolesanova²

Affiliations

¹ Institute of Biomedical Chemistry, 10/8, Pogodinskaya ul., Moscow, 119121, Russia.
² Institute of Biomedical Chemistry, 10/8, Pogodinskaya ul., Moscow, 119121, Russia. EKolesanova@yandex.ru.

^# Contributed equally.

PMID: 37450048
DOI: 10.1007/s00726-023-03302-4

Abstract

Polystyrene-based support Bio-Beads^® SM-2 was employed for desalting peptide-p-nitroanilides from Oxone^®. 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^® SM-2. Only unsubstituted phenyl-containing protection groups (carbobenzoxy or benzoyl) and Phe residues provided the adsorption of peptides on Bio-Beads^® SM-2 and their efficient desalting. This support is well suitable for multiple parallel phenyl group-containing peptide derivative separations and high-throughput screenings.

Keywords: Adsorption chromatography; Bio-Beads® SM-2; Desalting; Oxone®; Peptide-p-nitroanilides; Phenyl group.

Grants and funding

122030100170-5/Program for Basic Research in Russian Federation for a long-term period (2021-2030)