ISSN:
0003-3146
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
,
Physics
Notes:
Recent progresses in the elucidation of the folding mechanism and topology of proteins revealed that the formation of folding units with specific topological features is not restricted to a unique primary sequence. This finding presents the basis for the design of polypeptides having the propensity to fold into a tertiary structure that can be achieved by the assembly of peptide blocks exhibiting stable secondary structures. Conformational studies on model peptides show that Aib containing peptides with chain-lengths of 12-15 residues are able to form stable amphiphilic helices in solution. On the other hand, oligopeptides with alternating hydrophilic and hydrophobic residues are capable for β-structure formation for chain-lengths of 6-8 residues. Those amphiphilic secondary structures have been used as building-blocks for the design and synthesis of artificial folding units, their amphiphilic nature acting as major driving force for intramolecular folding. Spectroscopic data obtained for two polypeptides designed as βαβ-models actually suggest a folded conformation of these molecules in aqueous solution. The implications of these findings for the design of biologically active folded polypeptides are discussed.
Additional Material:
11 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/apmc.1986.051450112
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