scholarly journals Genetically Encoded Cyclic Peptide Phage Display Libraries

2020 ◽  
Vol 6 (3) ◽  
pp. 336-338 ◽  
Author(s):  
Leandro Simonetti ◽  
Ylva Ivarsson
2011 ◽  
Vol 75 (4) ◽  
pp. 812-815 ◽  
Author(s):  
Stefano ZANCONATO ◽  
Giovanni MINERVINI ◽  
Irene POLI ◽  
Davide De LUCREZIA

2005 ◽  
Vol 296 (1-2) ◽  
pp. 83-93 ◽  
Author(s):  
Jürgen W. Dieker ◽  
Yong-Jiang Sun ◽  
Cor W. Jacobs ◽  
Chaim Putterman ◽  
Marc Monestier ◽  
...  

1995 ◽  
Vol 92 (15) ◽  
pp. 7110-7114 ◽  
Author(s):  
F. R. DeLeo ◽  
L. Yu ◽  
J. B. Burritt ◽  
L. R. Loetterle ◽  
C. W. Bond ◽  
...  

2003 ◽  
Vol 307 (4) ◽  
pp. 791-796 ◽  
Author(s):  
Tamás Czömpöly ◽  
Árpád Lábadi ◽  
Mercedesz Balázs ◽  
Péter Németh ◽  
Péter Balogh

2017 ◽  
Vol 2017 ◽  
pp. 1-10 ◽  
Author(s):  
Juliana Seger Link ◽  
Silvana Maria Alban ◽  
Carlos Ricardo Soccol ◽  
Gilberto Vinicius Melo Pereira ◽  
Vanete Thomaz Soccol

This work’s goal was to research new candidate antigens for cutaneous leishmaniosis (CL). In order to reach the goal, we used random peptide phage display libraries screened using antibodies fromLeishmania braziliensispatients. After selection, three peptides (P1, P2, and P3) were synthesized using Fmoc chemistry. The peptides individually or a mixture of them (MIX) was subsequently emulsified in complete and incomplete Freund’s adjuvant and injected subcutaneously in golden hamsters. Sera from the hamsters administered with P1 presented antibodies that recognized proteins between 76 and 150 kDa fromL. braziliensis. Sera from hamsters which had peptides P2 and P3, as well as the MIX, administered presented antibodies that recognized proteins between 52 and 76 kDa ofL. braziliensis. The research on the similarity of the peptides’ sequences in protein databases showed that they match a 63 kDa glycoprotein. The three peptides and the MIX were recognized by the sera from CL patients by immunoassay approach (ELISA). The peptides’ MIX showed the best performance (79% sensitivity) followed by the P1 (72% sensitivity), and the AS presented 91% sensitivity. These results show a new route for discovering molecules for diagnosis or for immunoprotection against leishmaniosis.


2016 ◽  
Vol 62 (5) ◽  
pp. 481-495 ◽  
Author(s):  
G.A. Kuzmicheva ◽  
V.A. Belyavskaya

To date peptide phage display is one of the most common combinatorial methods used for identifying specific peptide ligands. Phage display peptide libraries containing billions different clones successfully used for selection of ligands with high affinity and selectivity toward wide range of targets including individual proteins, bacteria, viruses, spores, different kind of cancer cells and variety of nonorganic targets (metals, alloys, semiconductors etc.) Success of using filamentous phage in phage display technologies relays on the robustness of phage particles and a possibility to genetically modify its DNA to construct new phage variants with novel properties. In this review we are discussing characteristics of the most known non-commercial peptide phage display libraries of different formats (landscape libraries in particular) and their successful applications in several fields of biotechnology and biomedicine: discovery of peptides with diagnostic values against different pathogens, discovery and using of peptides recognizing cancer cells, trends in using of phage display technologies in human interactome studies, application of phage display technologies in construction of novel nano materials


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