How we drifted into peptide chemistry and where we have arrived at

Seebàch, Dieter; Kimmerlin, Thierry; Šebesta, Radovan; Campo, Marino A.; Beck, Albert K.

doi:10.1016/j.tet.2004.06.043

Cited by 117 publications

(49 citation statements)

References 674 publications

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“…The periodicity of this peptoid helix is three residues per turn, with a pitch of 6 Å [97] which is very similar to that of the 3 10 -helix. The other family of oligomers is the b-peptides [98,99], which differ from a-peptides by one additional backbone carbon atom. b-peptides composed of b 3 -L-amino acids are able to form left-handed 14-helices characterized by a periodicity of three residues per turn with a pitch of 4.7 Å , and H-bonds between the backbone amide proton of residue i and the carbonyl oxygen of residue i+2.…”

Section: Helical Foldamersmentioning

confidence: 99%

Development of small molecules designed to modulate protein–protein interactions

Che

Brooks

Marshall

2006

J Comput Aided Mol Des

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Protein-protein interactions are ubiquitous, essential to almost all known biological processes, and offer attractive opportunities for therapeutic intervention. Developing small molecules that modulate protein-protein interactions is challenging, owing to the large size of protein-complex interface, the lack of well-defined binding pockets, etc. We describe a general approach based on the "privileged-structure hypothesis" [Che, Ph.D. Thesis, Washington University, 2003] - that any organic templates capable of mimicking surfaces of protein-recognition motifs are potential privileged scaffolds as protein-complex antagonists--to address the challenges inherent in the discovery of small-molecule inhibitors of protein-protein interactions.

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Section: Helical Foldamersmentioning

confidence: 99%

Development of small molecules designed to modulate protein–protein interactions

Che

Brooks

Marshall

2006

J Comput Aided Mol Des

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“…[12,13] Investigations of b-peptides showed that they have an enormous potential for secondary structure formation, as documented in numerous comprehensive reviews. [14][15][16][17] The interest in this group of compounds stems from their antimicrobial applications; b-peptides containing b-amino acids occur very rarely in nature and they contain exclusively b-alanine derivatives. [1] Moreover, they form a more stable helix than a-peptides.…”

Section: Introductionmentioning

confidence: 99%

IR Low‐Temperature Matrix and ab Initio Study on β‐Alanine Conformers

et al. 2008

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For the first time the argon-matrix low-temperature FTIR spectra of beta-alanine are recorded. They reveal a quite complicated spectral pattern which suggests the presence of several beta-alanine conformers in the matrix. To interpret the spectra, the eighteen beta-alanine conformers, stable in the gas phase, are estimated at the B3LYP and MP2 levels combined with the aug-cc-pVDZ. Ten low-energy structures are reoptimized at the QCISD/aug-cc-pVDZ and B3LYP and MP2 levels by using the aug-cc-pVTZ basis sets. Assignment of the experimental spectra is undertaken on the basis of the calculated B3LYP/aug-cc-pVDZ anharmonic IR frequencies as well as careful estimation of the conformer population. The presence of at least three beta-alanine conformers is demonstrated. The detailed analysis of IR spectra points to the possible presence of five additional beta-alanine conformers.

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“…m-phenylene ethynylene (mPE) oligomers) (Scheme 4). [23,27,28] Among the many kinds of supramolecular hosts that have been reported in the literature over the past three decades, there are several key features that set the foldamer scaffold apart. As mentioned previously, many supramolecular host molecules require lengthy syntheses, and/or are limited in their ability to be unsymmetrically functionalized.…”

Section: Reactive Sieving With Foldamersmentioning

confidence: 99%

Reactive Sieving with Foldamers: Inspiration from Nature and Directions for the Future

Smaldone

Moore

2008

Chemistry A European J

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Over the past several decades, chemists have designed a myriad of supramolecular scaffolds for the purpose of mimicking enzyme behavior and creating more advanced catalysts. Foldamers, one class of supramolecular structures that feature rapid, modular synthesis and dynamic structural properties and have been widely investigated for their molecular recognition properties. Specifically, our group has designed a reactive m-phenyleneethynylene foldamer, which mimics the selective properties ("reactive sieving") of the isoleucine tRNA synthetase enzyme. In this concept we discuss examples that have inspired our research as well as potential directions for future advancement of this field.

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How we drifted into peptide chemistry and where we have arrived at

Cited by 117 publications

References 674 publications

Development of small molecules designed to modulate protein–protein interactions

Development of small molecules designed to modulate protein–protein interactions

IR Low‐Temperature Matrix and ab Initio Study on β‐Alanine Conformers

Reactive Sieving with Foldamers: Inspiration from Nature and Directions for the Future

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