Reaction medium engineering in enzymatic peptide fragment condensation : Synthesis of eledoisin and LH-RH
Björup, Peter ; Torres, Josep Lluís ; Adlercreutz, Patrick LU
and Clapés, Pere
(1998)
In Bioorganic and Medicinal Chemistry
6(7).
p.891-901
- Abstract
The influence of different reaction systems on α-chymotrypsin-catalyzed synthesis of eledoisin and LH-RH peptides from (7+4) and (5+5) fragments was investigated. The peptide yield was determined in the following systems: buffered aqueous media, frozen solutions, organic media, and cosolvent mixtures. The experimental set up was tailored to allow the screening of an array of conditions with minimum consumption of peptide fragments (2.1 and 2.5mM). The best yields (22% yield for eledoisin and 68% yield for LH-RH) were obtained in buffered aqueous solutions. It was found that the choice of buffer had a strong influence on the peptide yield; boric-borate and ammonium acetate buffers at pH 9, gave the best results. In buffered aqueous... (More)
The influence of different reaction systems on α-chymotrypsin-catalyzed synthesis of eledoisin and LH-RH peptides from (7+4) and (5+5) fragments was investigated. The peptide yield was determined in the following systems: buffered aqueous media, frozen solutions, organic media, and cosolvent mixtures. The experimental set up was tailored to allow the screening of an array of conditions with minimum consumption of peptide fragments (2.1 and 2.5mM). The best yields (22% yield for eledoisin and 68% yield for LH-RH) were obtained in buffered aqueous solutions. It was found that the choice of buffer had a strong influence on the peptide yield; boric-borate and ammonium acetate buffers at pH 9, gave the best results. In buffered aqueous systems, both syntheses were scaled up by using a 10-fold increase in fragment concentration (21 and 25mM). Under these conditions the yields rose to 57% and 80% of eledoisin and LH-RH, respectively. Moreover, during the synthesis of eledoisin and in the presence of boric-borate buffer pH 9, the peptide precipitated from the reaction medium preventing a secondary hydrolysis and facilitating the in situ product purification. Copyright (C) 1998 Elsevier Science Ltd.
(Less)
- author
- Björup, Peter
; Torres, Josep Lluís
; Adlercreutz, Patrick
LU
and Clapés, Pere
- organization
- publishing date
- 1998-07-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- α-chymotrypsin, Aqueous medium, Biologically active peptides, Cam esters, Eledoisin, Inverse substrate, Kinetically controlled fragment condensation, Luteinising hormone releasing hormone (LH-RH), Trypsin
- in
- Bioorganic and Medicinal Chemistry
- volume
- 6
- issue
- 7
- pages
- 11 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:2542508756
- pmid:9730225
- ISSN
- 0968-0896
- DOI
- 10.1016/S0968-0896(98)00046-7
- language
- English
- LU publication?
- yes
- id
- 438962d8-0c0c-4d4e-9bdd-1627c6b8eb6e
- date added to LUP
- 2019-06-20 16:04:23
- date last changed
- 2024-01-01 12:02:06
@article{438962d8-0c0c-4d4e-9bdd-1627c6b8eb6e,
abstract = {{<p>The influence of different reaction systems on α-chymotrypsin-catalyzed synthesis of eledoisin and LH-RH peptides from (7+4) and (5+5) fragments was investigated. The peptide yield was determined in the following systems: buffered aqueous media, frozen solutions, organic media, and cosolvent mixtures. The experimental set up was tailored to allow the screening of an array of conditions with minimum consumption of peptide fragments (2.1 and 2.5mM). The best yields (22% yield for eledoisin and 68% yield for LH-RH) were obtained in buffered aqueous solutions. It was found that the choice of buffer had a strong influence on the peptide yield; boric-borate and ammonium acetate buffers at pH 9, gave the best results. In buffered aqueous systems, both syntheses were scaled up by using a 10-fold increase in fragment concentration (21 and 25mM). Under these conditions the yields rose to 57% and 80% of eledoisin and LH-RH, respectively. Moreover, during the synthesis of eledoisin and in the presence of boric-borate buffer pH 9, the peptide precipitated from the reaction medium preventing a secondary hydrolysis and facilitating the in situ product purification. Copyright (C) 1998 Elsevier Science Ltd.</p>}},
author = {{Björup, Peter and Torres, Josep Lluís and Adlercreutz, Patrick and Clapés, Pere}},
issn = {{0968-0896}},
keywords = {{α-chymotrypsin; Aqueous medium; Biologically active peptides; Cam esters; Eledoisin; Inverse substrate; Kinetically controlled fragment condensation; Luteinising hormone releasing hormone (LH-RH); Trypsin}},
language = {{eng}},
month = {{07}},
number = {{7}},
pages = {{891--901}},
publisher = {{Elsevier}},
series = {{Bioorganic and Medicinal Chemistry}},
title = {{Reaction medium engineering in enzymatic peptide fragment condensation : Synthesis of eledoisin and LH-RH}},
url = {{http://dx.doi.org/10.1016/S0968-0896(98)00046-7}},
doi = {{10.1016/S0968-0896(98)00046-7}},
volume = {{6}},
year = {{1998}},
}