Abstract
Val5‐angiotensin‐I and one of its optical isomers, Val5‐D‐Phe8‐angiotensin‐I, were synthesized by a new way excluding any possibility of racemisation. The optical purity of the intermediary and final peptides was furthermore ascertained by enzymatic degradation. Val5‐angiotensin‐I exhibited the full biological activity expected. Val5‐D‐Phe8‐angiotensin‐I was found to be practically inactive. It failed also to antagonize Val5‐ or Ileu5‐angiotensin‐I or to inhibit «converting enzyme».

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