The introduction of a chlorine atom could potentially endow peptide derivatives with notable bioactivity and applicability. However, despite considerable recent progress in C(sp3)-H functionalization chemistry, a general method for the site-selective chlorination of inert aliphatic C-H bonds in peptides still remains elusive. Herein, we report a site-selective C(sp3)-H chlorination of oligopeptides based on an N-chloropeptide strategy. N-chloropeptides, which are easily prepared from the corresponding native oligopeptides, are smoothly degraded in the presence of an appropriate copper catalyst, and a subsequent 1,5-hydrogen atom transfer affords γ- or δ-chlorinated peptides in excellent yield. A wide variety of amino acid residues can thus be site-selectively chlorinated in a predictable manner. This method hence enables the efficient synthesis of otherwise less accessible, chlorine-containing peptide fragments of natural peptides. We moreover demonstrate here the successful estimation of the stereochemistry of the chlorinated carbon atom in aquimarin A. Furthermore, we reveal that side-chain-chlorinated peptides can serve as highly useful substructures with a fine balance between stability and reactivity, which renders them promising targets for synthetic and medicinal applications.