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Foldamers: Synthesis and Applications

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Organic Chemistry".

Deadline for manuscript submissions: closed (10 May 2017)

Special Issue Editor


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Guest Editor
Di.S.V.A. Chemistry, Polytechnic University of Marche, Via Brecce Bianche, I-60131 Ancona, Italy
Interests: conformationally restricted isosteres of natural amino acids; synthesis of cyclic monomers for foldamers via cyclofunctionalization reactions; design and preparation of novel atropisomers; α-hydrazido acids displaying significant antibiotic activity

Special Issue Information

Dear Colleagues,

Investigations concerning the protein folding led to development of compounds that were named “foldamers”. This definition deals with oligomers that display a secondary structure, mostly evidenced by spectroscopic methods, exploiting non-covalent interactions such as hydrogen bonding and aromatic stacking. Thus, a lot of different structures were obtained, although helices were most frequently observed. Moreover, it is worth mentioning that these compounds display interesting properties in disrupting protein–protein interactions, so that they are largely studied as drug candidates, being suitable for a novel approach to innovative therapeutics.

Prof. Dr. Mario Orena
Guest Editor

Manuscript Submission Information

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Keywords

  • Building blocks
  • β- and γ-peptides
  • De novo design
  • Aromatic foldamers
  • Pseudopeptides
  • Oligourea foldamers

Published Papers (1 paper)

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Research

1494 KiB  
Article
Distal Proton Shuttle Mechanism of Ribosome Catalysed Peptide Bond Formation—A Theoretical Study
by Xiaotong Zhang, Yafei Jiang, Qiuyun Mao, Hongwei Tan, Xichen Li, Guangju Chen and Zongchao Jia
Molecules 2017, 22(4), 571; https://doi.org/10.3390/molecules22040571 - 31 Mar 2017
Cited by 5 | Viewed by 4818
Abstract
In this work, we have investigated a novel distal proton shuttle mechanism of ribosome catalyzed peptide bond formation reaction. The reaction was found to follow a two-step mechanism. A distal water molecule located about 6.1 Å away from the attacking amine plays as [...] Read more.
In this work, we have investigated a novel distal proton shuttle mechanism of ribosome catalyzed peptide bond formation reaction. The reaction was found to follow a two-step mechanism. A distal water molecule located about 6.1 Å away from the attacking amine plays as a proton acceptor and results in a charge-separated intermediate that is stabilized by the N terminus of L27 and the A-site A76 5′-phosphate. The ribose A2451 bridges the proton shuttle pathway, thus plays critical role in the reaction. The calculated 27.64 kcal•mol−1 free energy barrier of the distal proton shuttle mechanism is lower than that of eight-membered ring transition state. The distal proton shuttle mechanism studied in this work can provide new insights into the important biological peptide synthesis process. Full article
(This article belongs to the Special Issue Foldamers: Synthesis and Applications)
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