Nucleic acids and polypeptides are at the heart of life.I ti si nteresting to ask whether the monomers of these biopolymers possess intrinsic reactivity that favors oligomerization in the absence of enzymes.W eh ave recently observed that covalently linked peptido RNAchains form when mixtures of monomers react in salt-rich condensation buffer.H ere,w e report the results of as creen of the 20 proteinogenic amino acids and four ribonucleotides.N one of the amino acids prevent phosphodiester formation, so all of them are compatible with genetic encoding through RNAc hain growth. A reactivity landscape was found, in whichp eptide formation strongly depends on the structure of the amino acid, but less on the nucleobase.F or example,p roline gives ribonucleotidebound peptides most readily,t yrosine favors pyrophosphate and phosphodiester formation, and histidine gives phosphorimidazolides as dominant products.When proline and aspartic acid were allowed to compete for incorporation, only proline was found at the N-terminus of peptido chains.T he reactivity described here links two fundamental classes of biomolecules through reactions that occur without enzymes,but with amino acid specificity.