Synthesis and structural stability of helichrome as an artificial hemeproteins.
A detailed procedure is described for the synthesis of helichrome, which is the first successful example of polypeptide-based artificial hemeprotein. The segment synthesis-condensation approach used for the assembly of small proteins has proven to be extremely useful for protein mimetics as well. The final deprotection was performed using the TMSOTf-thioanisole method instead of the less-convenient hydrogen fluoride method. The unfolding transition of the alpha-helical conformation of helichrome induced by guanidine hydrochloride was studied to understand the stability and dynamics of the folded structure. The resulting parameters (C0.5 = 5.2 M and delta GH2O = -4.4 kcal mol-1) characterizing helichrome denaturation were comparable to that of native globular proteins.
Sasaki
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Laboratory of Bioorganic Chemistry and Biochemistry, Rockefeller University, New York, New York 10021.
Kaiser
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D000595:Amino Acid Sequence; D006420:Hemeproteins / Q000378:metabolism; D008969:Molecular Sequence Data; D015394:Molecular Structure
D006420:Hemeproteins; C063808:helichrome