Most of the compounds have physiologically active properties, and their biological properties are often attributed to the heteroatoms contained in their molecules, and most of these heteroatoms also appear in cyclic structures. A Journal, Article, Research Support, U.S. Gov’t, Non-P.H.S., Research Support, U.S. Gov’t, P.H.S., Biopolymers called Synthesis and structural stability of helichrome as an artificial hemeproteins, Author is Sasaki, Tomikazu; Kaiser, Emil Thomas, which mentions a compound: 10466-61-2, SMILESS is N[C@@H](CC(C)C)C(N)=O.[H]Cl, Molecular C6H15ClN2O, Recommanded Product: H-Leu-NH2.HCl.
A detailed procedure is described for the synthesis of helichrome, which is the first successful example of polypeptide-based artificial hemeprotein. Boc-Ala-Glu(OCH2Ph)-Glu-Leu-Leu-Gln-Glu(OCH2Ph)-Leu-NH2 (Boc = Me3CO2C) was Boc-deblocked and then coupled with Boc-Ala-Glu(OCHiPh)-Glu-Leu-Leu-Glu-Glu(OCH2Ph)-OH by Me2N(CH2)3N:C:NEt.HCl/1-hydroxybenzotriazole to give Boc-Ala-Glu(OCH2Ph)-Glu-Leu-Leu-Gln-Glu(OCH2Ph)-Ala-Glu(OCH2Ph)-Glu-Leu-Leu-Glu-Glu(OCH2Ph)-Leu-NH2 (I). I was Boc-deblocked and coupled with the tetrasuccinimido ester of coproporphyrin I (II) to give the protected helichrome, which was deblocked by CF3SO3SiMe3/thioanisole to give the helichrome. The unfolding transition of the α-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 = 5.2M and ΔGH2O = 4.4 kcal mol-1) characterizing helichrome denaturation were comparable to that of native globular proteins.
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