Peptide synthesis. Part 8. A system for solid-phase synthesis under low pressure continuous flow conditions

Author(s):  
Alison Dryland ◽  
Robert C. Sheppard
1993 ◽  
Vol 58 (2) ◽  
pp. 435-444 ◽  
Author(s):  
Josef Vágner ◽  
Viktor Krchňák ◽  
Josef Pícha ◽  
Drahomíra Píchová ◽  
Martin Fusek

The synthesis of two medium-size peptide amides, the propart of human procathepsin D (1-45) and the bovine growth-hormon releasing factor (1-44) has been accomplished by the solid-phase multiple peptide synthesis under low-pressure continuous-flow conditions on standard methylbenzhydrylamine polystyrene-based resin in concatenated flow reactors with adjustable volume. The completeness of acylation of resin-bound free amino groups was monitored by the acid-base indicator bromophenol blue. The efficiency of the coupling reaction was increased by exposure to elevated temperature in an ultrasonic bath. Crude peptides were purified on a mass-overloaded Vydac C18 reversed-phase semipreparative HPLC column. The synthetic propart of human procathepsin D (1-45) exhibited inhibition activity to bovine cathepsin D and four other aspartic proteases. Significantly increased plasma concentration in gilts was determined after application of synthetic bovine growth-hormone releasing factor (1-44).


2020 ◽  
Author(s):  
yasmeen bakhatan ◽  
Israel Alshanski ◽  
Dana Grunhaus ◽  
Mattan Hurevich

Photocleavage from polystyrene beads is a pivotal reaction for solid phase synthesis that relies on photolabile linkers. The photocleavage, usually performed by batch irradiation, suffers from incomplete and slow cleavage. To overcome these issues, continuous flow and high-energy lamps are frequently used, but these setups are hazardous, technically challenging, and expensive. We developed a photocleavage approach that relies on a benchtop LED lamp and magnetic stirring. In this approach, we crush the beads instead of keeping their integrity to increase the yield of photocleavage. This approach proved very efficient for photocleavage of protected oligosaccharides.


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