The formation of terminated peptides with free α‐amino groups has often been observed in stepwise solid phase peptide synthesis. This has been attributed to variable accessibility in regions of the swollen crosslinked resin supports. It is now shown that impurities in the amino acid reagents are responsible for these by‐products. Thus,sec.‐butyloxycarbonylamino acids were isolated fromtert.‐butyloxycarbonylamino acids after treatment with trifluoroacetic acid under standard deprotection conditions for the removal of thetert.‐butyloxycarbonyl (Boc) group. Direct reverse phase HPLC analysis of Boc‐amino acids from commercial sources also showed thesec.‐Boc‐amino acids as impurities present at varying levels. Thesec.‐Boc group was stable to treatment at room temperature with trifluoroacetic acid in dichloromethane (1:1, v/v) (half‐life 7 years), but was removed by HF‐anisole under the standard conditions of cleavage and deprotection of assembled peptides. In model syntheses, the level of terminated free peptides corresponded to the level of preexistingsec.‐Boc‐amino acid impurities present in the Boc‐amino acid reagents. Use of Boc‐amino acids with no detectablesec.‐Boc resulted in negligible levels (<0.05%) of terminated peptides. The problem is thus readily overcome by the use of pure Boc‐amino acid starting materials and is not a reflection of a shortcoming inherent to the polymer supported nature of solid phase synthese