ISSN:
1435-1536
Keywords:
Reversed micelle
;
Basic poly(α-amino acid)s
;
Circular dichroism measurement
;
Conformational transition
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
,
Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
Notes:
Abstract The conformation of various basic poly (α-amino acid)s was investigated by CD measurements in aqueous solutions containing bis (2-ethylhexyl)sodium sulfosuccinate (AOT) as well as in the AOT reversed micelles. The addition of AOT into an aqueous solution of poly(L-lysine) induces the conformational transition from coil to ordered structure, followed by aggregation. On the other hand, poly(L-lysine) assumesΒ-structure in the reversed micelles at low wovalue (wo=[H2O]/[AOT]). Similarly to poly(L-lysine), poly(L-ornithine) takes an ordered structure in the aqueous solution containing AOT andΒ-structure in the reversed micelles. In this case, however, these ordered structures are not so stable, compared with that of poly(L-lysine). Poly(L-arginine) undergoes the conformational transition from coil to helix by addition of AOT into the aqueous solution. Further addition of AOT allows transformation intoΒ-structure. Copoly(L-lysyl-L-leucine) with 63% leucine residue was shown to take a stable helical conformation even in pure water. In the reversed micelles, however, this ordered structure is significantly changed probably because the hydrophobic interaction among the leucyl residues is lowered in the reversed micelles.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01451545
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