Chain conformation in polyretropeptides III: design of a 3(10) helix using alpha,alpha-dialkylated amino acids and retropeptide bonds.
Computer simulations have been used to design a polypeptide with a 3(10) helix conformation. The study has been been performed taking advantage of the intrinsic helix forming tendency of alpha-Aminoisobutyric acid. In order to avoid the formation of the alpha helix, which is the other common helical conformation adopted by alpha-Aminoisobutyric acid-based peptides, retropeptide bonds have been included in the sequence. Thus, retropeptides are not able to form the intramolecular hydrogen bonding interactions characteristic of the alpha helix. The influences of both the peptide length and the solvent have been examined and compared with those of the polypeptide without retropeptide bonds.
Alemán
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Departament d'Enginyería Química, E.T.S. d'Enginyers Industrials de Barcelona, Universitat Politécnica de Catalunya, Spain.
D000478:Alkylation; D000621:Aminoisobutyric Acids / Q000737:chemistry / Q000378:metabolism; D002251:Carbon Tetrachloride / Q000737:chemistry; D005740:Gases; D006860:Hydrogen Bonding; D008432:Mathematical Computing; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012996:Solutions; D012997:Solvents; D013816:Thermodynamics; D014867:Water
D000621:Aminoisobutyric Acids; D005740:Gases; D010455:Peptides; D012996:Solutions; D012997:Solvents; D014867:Water; C100049:2-aminoisobutyric acid; D002251:Carbon Tetrachloride