Stability of peptide amides under high pressure

• Verfasst von: Corrales Moreno, Margarita [VerfasserIn]
• Verfasst von: Fernández, Avelina [VerfasserIn]
• Verfasst von: Butz, Peter [VerfasserIn]
• Verfasst von: Stärke, Joachim [VerfasserIn]
• Verfasst von: Pfaff, E. [VerfasserIn]
• Verfasst von: Wiesmüller, K. H. [VerfasserIn]
• Verfasst von: Tauscher, Bernhard [VerfasserIn]
• Titel: Stability of peptide amides under high pressure
• Verf.angabe: M. Corrales, A. Fernández García, P. Butz, J. Stärke, E. Pfaff, K.H. Wiesmüller, B. Tauscher
• E-Jahr: 2007
• Jahr: 03 Apr 2007
• Umfang: 6 S.
• Fussnoten: Gesehen am 08.01.2024
• Titel Quelle: Enthalten in: High pressure research
• Ort Quelle: London [u.a.] : Taylor and Francis, 1988
• Jahr Quelle: 2007
• Band/Heft Quelle: 27(2007), 1, Seite 17-22
• ISSN Quelle: 1477-2299
• DOI: doi:10.1080/08957950601079801
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Cyclization
• Sach-SW: Deamidation
• Sach-SW: High hydrostatic pressure
• Sach-SW: Peptides
• K10plus-PPN: 1877462896

Abstract

The effects of pressure on two-model peptide amides have been analysed since the modifications in those groups are usually related to changes in protein/peptide functionality. Pressure accelerated the hydrolysis at the C-terminal amide of the dipeptide H-Leu-Gly-NH2, producing the diketopiperazine cLG that might have a biological role. Furthermore, pressure accelerated the deamidation of the asparagine residue in the oligopeptide H-Val-Pro-Gly-Val-Gly-Asn-Gly-Val-Pro-Gly-Val-Gly-OH containing an Asn-Gly sequence, probably via a cyclic imide intermediate, producing a peptide with aspartic acid. The reported pressure-induced modifications in amide groups were slow under the considered conditions (600-800 MPa, 60-80 °C). Effects under parameters closer to pressure-assisted thermal sterilization remain to be investigated.