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

NANOTUBES ARE FORMED BY SELF-ASSEMBLY OF ?-LACTALBUMIN MILK PROTEIN FOLLOWING A DIFFERENT ROUTE THAN ESTABLISHED FOR THE HYDROLYSIS WHICH INVOLVES V8 ENZYME, PHOSPHATE BUFFER AND APPROPRIATE AMOUNTS OF CALCIUM AT NEUTRAL PH. THE RESULTING NANOTUBES ARE USED AS TEMPLATES FOR THE GROWTH OF CONDUCTIVE SILVER NANOTUBES. TEM, SEM-EDS, AFM AND FTIR ARE USED FOR CHARACTERIZATION.