Open AccessSide‐chain control of β‐peptide secondary structures
Author(s) -
Martinek Tamás A.,
Fülöp Ferenc
Publication year - 2003
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1033.2003.03756.x
Subject(s) - side chain , peptide , folding (dsp implementation) , chemistry , protein secondary structure , chain (unit) , peptidomimetic , protein folding , beta sheet , amino acid , beta (programming language) , protein structure , protein tertiary structure , stereochemistry , polymer , biochemistry , organic chemistry , physics , computer science , astronomy , electrical engineering , programming language , engineering
As one of the most important families of non‐natural polymers with the propensity to form well‐defined secondary structures, the β‐peptides are attracting increasing attention. The compounds incorporating β‐amino acid residues have found various applications in medicinal chemistry and biochemistry. The conformational pool of β‐peptides comprises several periodic folded conformations, which can be classified as helices, and nonpolar and polar strands. The latter two are prone to form pleated sheets. The numerous studies that have been performed on the side‐chain dependence of the stability of the folded structures allow certain conclusions concerning the principles of design of the β‐peptide foldamers. The folding propensity is influenced by local torsional, side‐chain to backbone and long‐range side‐chain interactions. Although β‐peptide foldamers are sensitive to solvent, the systematic choice of the side‐chain pattern and spatiality allows the design of the desired specific secondary structure. The application of β‐peptide foldamers may open up new directions in the synthesis of highly organized artificial tertiary structures with biochemical functions.