Work

An Evaluation of Peptide‐Bond Isosteres

Year: 2011

Type: review

Abstract: Peptide-bond isosteres can enable a deep interrogation of the structure and function of a peptide or protein by amplifying or attenuating particular chemical properties. In this Minireview, the electronic, structural, and conformational attributes of four such isosteres-thioamides, esters, alkenes, and fluoroalkenes-are examined in detail. In particular, the ability of these isosteres to partake in noncovalent interactions is compared with that of the peptide bond. The consequential perturbations provide a useful tool for chemical biologists to reveal new structure-function relationships, and to endow peptides and proteins with desirable attributes.

Source: ChemBioChem

DOI: 10.1002/cbic.201100272

Authors: Amit Choudhary, Ronald T. Raines

Institution: University of Wisconsin–Madison

Language: English

Topic: Chemical Synthesis and Analysis

Subfield: Organic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Institutes of Health, National Cancer Institute, National Institute of General Medical Sciences, National Institute of Arthritis and Musculoskeletal and Skin Diseases

Awards: Protein Chemistry, Chemistry and Biology of Collagen, Human Ribonuclease as a Cytotoxin