Molecular Pom Poms from Self-Assembling α,γ-Cyclic Peptides

2014 ◽  
Vol 20 (33) ◽  
pp. 10260-10265 ◽  
Author(s):  
Michele Panciera ◽  
Manuel Amorín ◽  
Juan R. Granja
2006 ◽  
Vol 110 (38) ◽  
pp. 18965-18972 ◽  
Author(s):  
Ekta Khurana ◽  
Steven O. Nielsen ◽  
Bernd Ensing ◽  
Michael L. Klein

2017 ◽  
Vol 19 (29) ◽  
pp. 19032-19042 ◽  
Author(s):  
Z. Faidon Brotzakis ◽  
Mascha Gehre ◽  
Ilja K. Voets ◽  
Peter G. Bolhuis

From right to left: three distinct growth mechanisms of a pentamer to a hexamer putative antifreeze cyclic peptide nanotube.


2018 ◽  
Vol 9 (43) ◽  
pp. 8228-8233 ◽  
Author(s):  
Alejandro Lamas ◽  
Arcadio Guerra ◽  
Manuel Amorín ◽  
Juan R. Granja

Here we show that 4-aminocyclohexanecarboxylic acid is a rigid stretcher building block for the preparation of cyclic peptides that self-assemble to form peptide nanotubes with large diameter and hydrophobic pores.


Soft Matter ◽  
2018 ◽  
Vol 14 (30) ◽  
pp. 6320-6326 ◽  
Author(s):  
Edward D. H. Mansfield ◽  
Matthias Hartlieb ◽  
Sylvain Catrouillet ◽  
Julia Y. Rho ◽  
Sophie C. Larnaudie ◽  
...  

Self-assembling cyclic peptides (CP) consisting of amino acids with alternating d- and l-chirality form nanotubes by hydrogen bonding, hydrophobic interactions, and π–π stacking in solution.


2014 ◽  
Vol 50 (6) ◽  
pp. 688-690 ◽  
Author(s):  
Manuel Amorín ◽  
Ana Pérez ◽  
Joaquín Barberá ◽  
Haxel Lionel Ozores ◽  
José Luis Serrano ◽  
...  

2012 ◽  
Vol 10 (44) ◽  
pp. 8762 ◽  
Author(s):  
Arcadio Guerra ◽  
Roberto J. Brea ◽  
Manuel Amorín ◽  
Luis Castedo ◽  
Juan R. Granja

2016 ◽  
Vol 7 (1) ◽  
pp. 183-187 ◽  
Author(s):  
Nuria Rodríguez-Vázquez ◽  
Rebeca García-Fandiño ◽  
Manuel Amorín ◽  
Juan R. Granja

The design and synthesis of self-assembling cyclic peptides with tunable cavity properties is described, allowing the incorporation of guests with different features.


2021 ◽  
Vol 9 ◽  
Author(s):  
Alexandre Blanco-González ◽  
Martín Calvelo ◽  
Pablo F. Garrido ◽  
Manuel Amorín ◽  
Juan R. Granja ◽  
...  

Self-assembling cyclic peptide nanotubes have been shown to function as synthetic, integral transmembrane channels. The combination of natural and nonnatural aminoacids in the sequence of cyclic peptides enables the control not only of their outer surface but also of the inner cavity behavior and properties, affecting, for instance, their permeability to different molecules including water and ions. Here, a thorough computational study on a new class of self-assembling peptide motifs, in which δ-aminocycloalkanecarboxylic acids are alternated with natural α-amino acids, is presented. The presence of synthetic δ-residues creates hydrophobic regions in these α,δ-SCPNs, which makes them especially attractive for their potential implementation in the design of new drug or diagnostic agent carrier systems. Using molecular dynamics simulations, the behavior of water molecules, different ions (Li+, Na+, K+, Cs+, and Ca2+), and their correspondent counter Cl− anions is extensively investigated in the nanoconfined environment. The structure and dynamics are mutually combined in a diving immersion inside these transmembrane channels to discover a fascinating submarine nanoworld where star-shaped water channels guide the passage of cations and anions therethrough.


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