Dynamics of energy transfer in peptide - Surface collisions

Oussama Meroueh, William L. Hase

Research output: Contribution to journalArticlepeer-review

82 Scopus citations


Classical trajectory simulations are performed to study energy transfer in collisions of protonated triglycine (Gly)3 and pentaglycine (Gly)5 ions with n-hexyl thiolate self-assembled monolayer (SAM) and diamond {111} surfaces, for a collision energy Ei in the range of 10-110 eV and a collision angle of 45°. Energy transfer to the peptide ions' internal degrees of freedom is more efficient for collision with the diamond surface; i.e., 20% transfer to peptide vibration/rotation at Ei = 30 eV. For collision with diamond, the majority of Ei remains in peptide translation, while the majority of the energy transfer is to surface vibrations for collision with the softer SAM surface. The energy-transfer efficiencies are very similar for (Gly)3 and (Gly)5. Constraining various modes of (Gly)3 shows that the peptide torsional modes absorb ∼80% of the energy transfer to the peptide's internal modes. The energy-transfer efficiencies depend on Ei. These simulations are compared with recent experiments of peptide SID and simulations of energy transfer in Cr(CO)6+ collisions with the SAM and diamond surfaces.

Original languageEnglish
Pages (from-to)1524-1531
Number of pages8
JournalJournal of the American Chemical Society
Issue number7
StatePublished - Feb 20 2002


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