scholarly journals Unusually high α-proton acidity of prolyl residues in cyclic peptides

2020 ◽  
Vol 11 (29) ◽  
pp. 7722-7729
Author(s):  
Oliver R. Maguire ◽  
Bethany Taylor ◽  
Eleanor M. Higgins ◽  
Matthew Rees ◽  
Steven L. Cobb ◽  
...  
Keyword(s):  
Cyclic Peptides ◽  
Computational Studies ◽  
Stereoelectronic Effect

Kinetic and computational studies reveal that prolyl residues in cyclic peptides are substantially more acidic than other residues due to a stereoelectronic effect.

Discovery and applications of naturally occurring cyclic peptides

Planta Medica ◽  
2011 ◽  
Vol 77 (12) ◽  
Author(s):  
D Craik ◽  
A Poth ◽  
M Colgrave ◽  
M Akcan ◽  
B Oku ◽  
...  
Keyword(s):  
Cyclic Peptides ◽  
Naturally Occurring

Biosynthetic origin of N-methyl-3-(3-furyl)-alanine in cyclic peptides produced by Stachylidium sp

Planta Medica ◽  
2014 ◽  
Vol 80 (16) ◽  
Author(s):  
F El Maddah ◽  
M Nazir ◽  
S Kehraus ◽  
GM König
Keyword(s):  
Cyclic Peptides

Computational Studies of Human Motion: Part 1, Tracking and Motion Synthesis

2005 ◽  
Author(s):  
David A. Forsyth ◽  
Okan Arikan ◽  
Leslie Ikemoto ◽  
James O'Brien ◽  
Deva Ramanan
Keyword(s):  
Human Motion ◽  
Computational Studies ◽  
Motion Synthesis

Experimental and Computational Studies of the Relative Flow Field in a Centrifugal Blood Pump

2000 ◽  
Vol 28 (1-2) ◽  
pp. 119-125 ◽  
Author(s):  
B. T. H. Ng ◽  
Weng Kong Chan ◽  
S. C. M. Yu ◽  
HaiDong Li
Keyword(s):  
Flow Field ◽  
Blood Pump ◽  
Computational Studies ◽  
Centrifugal Blood Pump ◽  
Relative Flow

Computational studies of hard-body and 3-D effects in plume flows

1989 ◽  
Author(s):  
ETHIRAJ VENKATAPATHY ◽  
WILLIAM FEIEREISEN ◽  
SHIGERU OBAYASHI
Keyword(s):  
Computational Studies ◽  
Plume Flows

Target-Templated de novo Design of Macrocyclic D-/L-Peptides: Inhibitors of the PD-1/PD-L1 Interaction

2020 ◽  
Author(s):  
Salvador Guardiola ◽  
Monica Varese ◽  
Xavier Roig ◽  
Jesús Garcia ◽  
Ernest Giralt
Keyword(s):  
Protein Interactions ◽  
Cyclic Peptides ◽  
General Framework ◽  
Large Scale ◽  
De Novo ◽  
Inhibitory Effect ◽  
Original Text ◽  
Protein Protein Interactions ◽  
Retraction Notice ◽  
Pharmaceutical Properties

<p>NOTE: This preprint has been retracted by consensus from all authors. See the retraction notice in place above; the original text can be found under "Version 1", accessible from the version selector above.</p><p><br></p><p>------------------------------------------------------------------------</p><p><br></p><p>Peptides, together with antibodies, are among the most potent biochemical tools to modulate challenging protein-protein interactions. However, current structure-based methods are largely limited to natural peptides and are not suitable for designing target-specific binders with improved pharmaceutical properties, such as macrocyclic peptides. Here we report a general framework that leverages the computational power of Rosetta for large-scale backbone sampling and energy scoring, followed by side-chain composition, to design heterochiral cyclic peptides that bind to a protein surface of interest. To showcase the applicability of our approach, we identified two peptides (PD-<i>i</i>3 and PD-<i>i</i>6) that target PD-1, a key immune checkpoint, and work as protein ligand decoys. A comprehensive biophysical evaluation confirmed their binding mechanism to PD-1 and their inhibitory effect on the PD-1/PD-L1 interaction. Finally, elucidation of their solution structures by NMR served as validation of our <i>de novo </i>design approach. We anticipate that our results will provide a general framework for designing target-specific drug-like peptides.<i></i></p>

Sign in / Sign up

Export Citation Format

Share Document