Intense femtosecond laser pulses, judiciously tailored in an adaptive, optimal control feedback loop were used to break preferentially the acyl-N (peptide) bond of Ac-Phe-NHMe that may be regarded as a dipeptide model. We show that coherent excitation of complex wave packets in the strong-field regime allows to cleave strong backbone bonds in the molecular system preferentially, while keeping other more labile bonds intact. These results show the potential of pulse shaping as a powerful complementary analytical tool for protein sequencing of large biopolymers in addition to the well-known mass spectrometry and chemical analysis. (c) 2007 American Institute of Physics.
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