ISSN:
0006-3592
Schlagwort(e):
enzymatic peptide synthesis
;
N-terminal protecting groups
;
α-chymotrypsin
;
experimental design
;
partition constant
;
reaction rate
;
log P
;
molecular refractivity
;
response surfaces
;
Chemistry
;
Biochemistry and Biotechnology
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Biologie
,
Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
Notizen:
The influence of five different N-terminal protecting groups (For, Ac, Boc, Z, and Fmoc) and reaction conditions (temperature and dimethylformamide content) on the α-chymotrypsin-catalyzed synthesis of the dipeptide derivative X-Phe-Leu-NH2 was studied. Groups such as For, Ac, Boc, and Z always rendered good peptide yields (82% to 85%) at low reaction temperatures and DMF concentrations, which depended on the N-α protection choice. Boc and Z were the most reactive N-α groups and, in addition, the most suitable for peptide synthesis. On the other hand, the use of empirical design methodologies allowed, with minimal experimentation and by multiple regression, to deduce an equation, which correlates the logarithm of the first order kinetic constant (log k') with reaction temperature, DMF concentration, and hydrophobicity (log P values) of the different protecting groups. The predictive value of the equation was tested by comparing the performance of another protective group, such as Aloc, with the performance predicted by said equation. Experimental and calculated k' values were found to be in good agreement.
Zusätzliches Material:
5 Ill.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1002/bit.260390509
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