A continued study of structural modification of S-trityl-L-cysteine reveals that for antileukemic activity, steric requirements of the trityl position appear to be more important than consideration of electron localization, hydrocarbon activity, or free radical stability. Activity of certain S-trityl-L-cysteinyl amino acids is observed but is of lesser degree than that of the parent S-trityl-L-cysteine. N-Substituted dipeptides and derivatives of S-trityl-L-cysteine are devoid of activity. Monohydroxymethyl-substituted S-trityl-L-cysteine still retains the original activity whereas the corresponding bis(hydroxymethyl) analog is inactive.

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6,7‐Dimethoxy‐2‐naphthylethylamine, prepared by the diborane reduction of 6,7‐dimethoxy‐2‐naphtlialeneacetamide, underwent a Pictet‐Spengler cyclization to form 8,9‐dimethoxy‐1,2,3,4‐tetrahydrobenz[h]isoquinoline. This compound is identical with that obtained by reduction of the corresponding dihydrobenzisoquinoline prepared from formamide cyclization. 6,7‐Dialkoxy‐2‐naphthaleneacetic acids, the key intermediates for the preparation of these amides, were obtained from 6,7‐dialkoxy‐2‐acetonaphthones by a modified Willgerodt reaction.