Stability of peptide amides under high pressure
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 c...
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| Hauptverfasser: | , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
03 Apr 2007
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| In: |
High pressure research
Year: 2007, Jahrgang: 27, Heft: 1, Pages: 17-22 |
| ISSN: | 1477-2299 |
| DOI: | 10.1080/08957950601079801 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1080/08957950601079801
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| Verfasserangaben: | M. Corrales, A. Fernández García, P. Butz, J. Stärke, E. Pfaff, K.H. Wiesmüller, B. Tauscher |
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| 520 | |a 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. | ||
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| 650 | 4 | |a High hydrostatic pressure | |
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