Measurement of the Length of the α Helical Section of a Peptide Directly Using Atomic Force Microscopy

概要

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Using atomic force microscopy(AFM), the length of the α-helix structure of poly-L-lysine was investigated by stretching the peptide directly, one molecule at a time. In the absence of urea, many rupturing points that seemed to be due to the breaking of some hydrogen bonds were observd in force-extension curves, while these points were never observed in he presence of 8M urea. In the presence of 0.4 or 1.6M urea, both force-extension curve types were observed. Total peptide elongation for each condition was calculated from force-extention curves reflecting the α-helix rupturing process. The experimental value of total elongation divided by the theoretical value of total α-helix elongaion yields the α-helix content. This value was compatible with circular dichroism(CD) measurement results. This suggests that peptide conformaion and content of the α-helix on a single molecule scale can be investigated by direct mechanical measuerment using atomic force microscopy.
公益社団法人日本薬学会の論文
2001-12-01