scholarly journals Oligopeptide M13 Phage Display in Pathogen Research

Viruses ◽  
2013 ◽  
Vol 5 (10) ◽  
pp. 2531-2545 ◽  
Author(s):  
Jonas Kügler ◽  
Jonas Zantow ◽  
Torsten Meyer ◽  
Michael Hust
Keyword(s):  
Molecules ◽  
2011 ◽  
Vol 16 (2) ◽  
pp. 1211-1239 ◽  
Author(s):  
Tek N. Lamichhane ◽  
N. Dinuka Abeydeera ◽  
Anne-Cécile E. Duc ◽  
Philip R. Cunningham ◽  
Christine S. Chow

Immunology ◽  
1996 ◽  
Vol 88 (4) ◽  
pp. 482-486 ◽  
Author(s):  
M. P. DAVENPORT ◽  
C. L. QUINN ◽  
P. VALSASNINI ◽  
F. SINIGAGLIA ◽  
A. V. S. HILL ◽  
...  

2008 ◽  
Vol 373 (1) ◽  
pp. 88-98 ◽  
Author(s):  
Leighanne A. Brammer ◽  
Benjamin Bolduc ◽  
Jessica L. Kass ◽  
Kristin M. Felice ◽  
Christopher J. Noren ◽  
...  

1999 ◽  
Vol 380 (1) ◽  
Author(s):  
L. Kiczak ◽  
K. Koscielska ◽  
J. Otlewski ◽  
M. Czerwinski ◽  
M. Dadlez

AbstractThe P1 position of protein inhibitors and oligopeptide substrates determines, to a large extent, association energy with many serine proteinases. To test the agreement of phage display selection with the existing thermodynamic data, a small library of all 20 P1 mutants of basic pancreatic trypsin inhibitor (BPTI) was created, fused to protein III, and displayed on the surface of M13 phage. The wild type of displayed inhibitor monovalently and strongly inhibited trypsin with an association constant of


Molecules ◽  
2011 ◽  
Vol 16 (2) ◽  
pp. 1667-1681 ◽  
Author(s):  
Yuliya Georgieva ◽  
Zoltán Konthur

2012 ◽  
Vol 59 (6) ◽  
pp. 490-494 ◽  
Author(s):  
L'ubomíra Tóthová ◽  
Janka Bábíčková ◽  
Peter Celec
Keyword(s):  

2014 ◽  
Vol 14 (1) ◽  
pp. 12 ◽  
Author(s):  
Martin Ploss ◽  
Sandra J Facey ◽  
Carina Bruhn ◽  
Limor Zemel ◽  
Kathrin Hofmann ◽  
...  

2019 ◽  
Author(s):  
Jasmim Leal ◽  
Tony Dong ◽  
Feng Gao ◽  
Melissa Soto ◽  
Hugh D.C. Smyth ◽  
...  

ABSTRACTMucus is an impregnable barrier for drug delivery across the epithelia for treatment of mucosal-associated diseases. While current carriers are promising for mucus penetration, their surface chemistries do not possess chemical complexity to probe and identify optimal physicochemical properties desired for mucus penetration. As initial study, we use M13 phage display presenting random peptides to select peptides that can facilitate permeation through hyperconcentrated mucin. Here, a net-neutral charge, hydrophilic peptide was identified to facilitate transport of phage and fluorophore conjugates through mucin barrier compared to controls. This initial finding warrants further study to understand how composition and spatial distribution of physicochemical properties of peptides can be optimized to improve transport across the mucus barrier.


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