Application of the continuous-flow polyamide method to the solid-phase synthesis of a multiple antigen peptide (MAP) based on the sequence of a malaria epitope

1990 ◽  
pp. 8 ◽  
Author(s):  
Antonello Pessi ◽  
Elisabetta Bianchi ◽  
Fabio Bonelli ◽  
Lorella Chiappinelli
Keyword(s):  
Continuous Flow ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Phase Synthesis ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Peptide Map

scholarly journals The Breaking Beads Approach for Photocleavage from Solid Support

2020 ◽  
Author(s):  
yasmeen bakhatan ◽  
Israel Alshanski ◽  
Dana Grunhaus ◽  
Mattan Hurevich
Keyword(s):  
Continuous Flow ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
High Energy ◽  
Solid Support ◽  
Phase Synthesis ◽  
Polystyrene Beads ◽  
Magnetic Stirring ◽  
Photolabile Linkers

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.

scholarly journals Antimicrobial Activity of Novel Dendrimeric Peptides Obtained by Phage Display Selection and Rational Modification

2005 ◽  
Vol 49 (7) ◽  
pp. 2665-2672 ◽  
Author(s):  
Alessandro Pini ◽  
Andrea Giuliani ◽  
Chiara Falciani ◽  
Ylenia Runci ◽  
Claudia Ricci ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Multidrug Resistant ◽  
Cytotoxic Effects ◽  
E Coli ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Residue Substitution ◽  
Peptide Map ◽  
Phage Peptide Library

ABSTRACT A large 10-mer phage peptide library was panned against whole Escherichia coli cells, and an antimicrobial peptide (QEKIRVRLSA) was selected. The peptide was synthesized in monomeric and dendrimeric tetrabranched form (multiple antigen peptide [MAP]), which generally allows a dramatic increase of peptide stability to peptidases and proteases. The antibacterial activity of the dendrimeric peptide against E. coli was much higher than that of the monomeric form. Modification of the original sequence, by residue substitution or sequence shortening, produced three different MAPs, M4 (QAKIRVRLSA), M5 (KIRVRLSA), and M6 (QKKIRVRLSA) with enhanced stability to natural degradation and antimicrobial activity against a large panel of gram-negative bacteria. The MICs of the most potent peptide, M6, were as low as 4 to 8 μg/ml against recent clinical isolates of multidrug-resistant Pseudomonas aeruginosa and members of the Enterobacteriaceae. The same dendrimeric peptides showed high stability to blood proteases, low hemolytic activity, and low cytotoxic effects on eukaryotic cells, making them promising candidates for the development of new antibacterial drugs.

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