Asymmetric catalysis mediated by synthetic peptides, version 2.0: expansion of scope and mechanisms

AJ Metrano, AJ Chinn, CR Shugrue, EA Stone… - Chemical …, 2020 - ACS Publications
Low molecular weight synthetic peptides have been demonstrated to be effective catalysts
for an increasingly wide array of asymmetric transformations. In many cases, these peptide …

Structure‐based design of inhibitors of protein–protein interactions: mimicking peptide binding epitopes

M Pelay‐Gimeno, A Glas, O Koch… - Angewandte Chemie …, 2015 - Wiley Online Library
Protein–protein interactions (PPIs) are involved at all levels of cellular organization, thus
making the development of PPI inhibitors extremely valuable. The identification of selective …

Peptidic foldamers: ramping up diversity

TA Martinek, F Fülöp - Chemical Society Reviews, 2012 - pubs.rsc.org
Non-natural folded polymers (foldamers) display considerable versatility, and the design of
such molecules is of great current interest. In this respect, peptidic foldamers are perhaps …

Foldamers as versatile frameworks for the design and evolution of function

CM Goodman, S Choi, S Shandler… - Nature chemical …, 2007 - nature.com
Foldamers are sequence-specific oligomers akin to peptides, proteins and oligonucleotides
that fold into well-defined three-dimensional structures. They offer the chemical biologist a …

The World of β‐ and γ‐Peptides Comprised of Homologated Proteinogenic Amino Acids and Other Components

D Seebach, AK Beck, DJ Bierbaum - Chemistry & biodiversity, 2004 - Wiley Online Library
The origins of our nearly ten‐year research program of chemical and biological
investigations into peptides based on homologated proteinogenic amino acids are …

Foldamers with heterogeneous backbones

WS Horne, SH Gellman - Accounts of chemical research, 2008 - ACS Publications
The functions performed by proteins and nucleic acids provide the foundation for life.
Chemists have recently begun to ask whether it is possible to design synthetic oligomers …

Structural chemistry of peptides containing backbone expanded amino acid residues: conformational features of β, γ, and hybrid peptides

PG Vasudev, S Chatterjee, N Shamala… - Chemical …, 2011 - ACS Publications
The remarkable complexity of globular protein structures was first revealed about half a
century ago, when the crystal structure of myoglobin was determined at 2.4 Å. 1 In the …

Interplay among folding, sequence, and lipophilicity in the antibacterial and hemolytic activities of α/β-peptides

MA Schmitt, B Weisblum… - Journal of the American …, 2007 - ACS Publications
Host-defense peptides inhibit bacterial growth but manifest relatively little toxicity toward
eukaryotic cells. Many host-defense peptides adopt α-helical conformations in which …

Helix bundle quaternary structure from α/β-peptide foldamers

WS Horne, JL Price, JL Keck… - Journal of the American …, 2007 - ACS Publications
The function of a protein generally depends on adoption of a specific folding pattern, which
in turn is determined by the side chain sequence along the polypeptide backbone. Here we …

Unexpected relationships between structure and function in α, β-peptides: antimicrobial foldamers with heterogeneous backbones

MA Schmitt, B Weisblum… - Journal of the American …, 2004 - ACS Publications
We describe our first effort to design antimicrobial α/β-peptides based upon their helical
folding behavior. α/β-Peptide 3 (above), designed as a scrambled negative control …