Binding loop of sunflower trypsin inhibitor 1 serves as a design motif for proteolysis-resistant antimicrobial peptides

Author(s):  
Chensi Wang ◽  
Changxuan Shao ◽  
Yuxin Fang ◽  
Jiajun Wang ◽  
Na Dong ◽  
...  
2000 ◽  
Vol 295 (5) ◽  
pp. 1237-1249 ◽  
Author(s):  
Honorata Czapinska ◽  
Jacek Otlewski ◽  
Szymon Krzywda ◽  
George M Sheldrick ◽  
Mariusz Jaskólski

FEBS Letters ◽  
1998 ◽  
Vol 436 (2) ◽  
pp. 174-178 ◽  
Author(s):  
Anna Jaśkiewicz ◽  
Katarzyna Lis ◽  
Jan Różycki ◽  
Gotfryd Kupryszewski ◽  
Krzysztof Rolka ◽  
...  

Synlett ◽  
2017 ◽  
Vol 28 (15) ◽  
pp. 1901-1906 ◽  
Author(s):  
Christian Tornøe ◽  
Eva Johansson ◽  
Per-Olof Wahlund

A divergent protein synthesis strategy was executed to effectively synthesize Bowman–Birk protease inhibitor (BBI) analogues using native chemical ligation of peptide hydrazides. Grafting selected residues from a potent trypsin inhibitor, sunflower trypsin inhibitor-1, onto the α-chymotrypsin-binding loop of BBI, resulted in a fourfold improvement of α-chymotrypsin inhibition. The crystal structure of a synthetic BBI analogue co-crystallized with α-chymotrypsin confirmed the correct protein fold and showed a similar overall structure to unmodified BBI in complex with α-chymotrypsin. Dynamic light scattering showed that C-terminal truncation of BBI led to increased self-association.


Pneumologie ◽  
2009 ◽  
Vol 63 (S 01) ◽  
Author(s):  
G Günther ◽  
E Andresen ◽  
J Bullwinkel ◽  
C Lange ◽  
H Heine

2009 ◽  
Vol 47 (06) ◽  
Author(s):  
B Diaconu ◽  
A Schneider ◽  
R Pfützer ◽  
T Mocan ◽  
M Scăfaru ◽  
...  

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