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Synthetic Studies of Structure-Function Relationships in Staphylococcal Nuclease

SYNTHETIC ANALOGUES OF FRAGMENT P₂

From the ¹ From the Laboratory of Chemical Biology, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland 20014

The solid phase technique of peptide synthesis has been used to study structural features related to the activity of Fragment P₂ (Residues 6 through 48) of nuclease-T. Binding of synthetic analogues to the complimentary native Fragment P₃ (Residues 49 through 149) may be detected by affinity chromatography upon an agarose column containing covalently bound P₃. Binding in free solution was detected by changes in the fluorescence spectrum of the single tryptophan residue in P₃. Previous studies have shown that the synthetic 6-47 peptide, after purification by specific binding to an agarose P₃ column, can generate approximately 30% of the maximum enzymic activity when added in an equivalent molar quantity to Fragment P₃

Deletion of the NH₂-terminal tripeptide from synthetic P₂ (yielding synthetic 9-47) leaves both binding and activating abilities intact. Two shorter analogues, synthetic 18-47 and synthetic 33-47, have no activity, although the 18-47 analogue appears to retain some binding affinity for native P₃.

The methionine residues at positions 26 and 32 may be replaced by norleucine to give an analogue capable of both binding to and activating P₃. Replacement of glutamic acid by glutamine at position 43 leads to an inactive derivative which retains its ability to bind specifically to Fragment P₃.

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