Peptide Bond Isosteres:  Ester or (E)-Alkene in the Backbone of the Collagen Triple Helix

Collagen is the most abundant protein in animals. Interstrand N−H···OC hydrogen bonds between backbone amide groups form a ladder in the middle of the collagen triple helix. Isosteric replacement of the hydrogen-bond-donating amide with an ester or (E)-alkene markedly decreases the conformational s...

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Bibliographic Details
Published in:Organic letters 2005-06, Vol.7 (13), p.2619-2622
Main Authors: Jenkins, Cara L, Vasbinder, Melissa M, Miller, Scott J, Raines, Ronald T
Format: Article
Language:English
Subjects:
Alkenes - chemistry
Amino Acid Sequence
Collagen - chemistry
Esters
Hydrogen Bonding
Models, Molecular
Molecular Structure
Protein Conformation
Stereoisomerism
Thermodynamics
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Summary:Collagen is the most abundant protein in animals. Interstrand N−H···OC hydrogen bonds between backbone amide groups form a ladder in the middle of the collagen triple helix. Isosteric replacement of the hydrogen-bond-donating amide with an ester or (E)-alkene markedly decreases the conformational stability of the triple helix. Thus, this recurring hydrogen bond is critical to the structural integrity of collagen. In this context, an ester isostere confers more stability than does an (E)-alkene.
ISSN:1523-7060
1523-7052
DOI:10.1021/ol050780m