In this work, we report systematic surface-enhanced Raman spectroscopy (SERS) and generalized two-dimensional correlation analysis (G2DCA) studies of the structures of five specifically modified phenylatanine-substituted C-terminal bombesin 6-14 fragments (BN6-14). The fragments studied have all been tested as chemotherapeutic agents in cancer therapy, and they form amino acid sequences in bombesin: cyclol[D)-Phe(6), His(7),Leu(14)], BN6-14, [D-Phe(6), Leu-NHEt13,des-Met(14)] BN6-14, [D-Phe(6) Leu(13)-((R))-p-Cl-Phe(14)] BN6-14, [D-Phe(6),beta-Ala(11),Phe(13),Nle(14)]BN6-14, and [D-Tyr(6),beta-Ala(11),Phe(13),Nle(14)]BN6-14. We adsorbed these fragments onto roughened Ag, Au, and Cu electrode surfaces, using a potential range from -1.200 to 0.400 V, at physiological pH. We compared the adsorption mechanism of each fragment on these substrates, as well any changes observed with varying electrode potential, to determine the relationship between adsorption strength and geometry of each of the peptides wherever it was possible. For example, we showed that none of these fragments directly interact with the Ag, Au, and Cu surfaces via residues of Phe (phenylaianine) and Trp(8) (L-tryptophane at position 8 of the BN amino acid sequence) or by an amide bond, due to a very small shift in wavenumber of their characteristic vibrations. Specific interactions were recognized from the broadening, wavenumber shift, and increase in intensity of the W18 Trp(8) mode near 759 cm(-1) and decrease in v(12) vibration frequency of the Phe residue. In general, more intense SERS bands were observed due to the Phe ring, compared with the Trp(8) ring, which suggested a preferential adsorption of phenylalanine over tryptophane. For [D-Tyr(6),beta-Ala(11),Phe(13) ,Nle(14)]BN6-14, the data also suggest some interaction of a D-Tyr(6) residue (D-tyrosine at position 6). Finally, only slight rearrangements of these moieties on the substrates are observed with changes in electrode potential.