Anomalous temperature fluorescence quenching of N-Trp terminal peptides.
The photophysics of Trp-containing peptides is extremely affected by the position of the indole ring with respect to substituents. In this work an unusual temperature fluorescence quenching behavior is presented. The N-tryptophan terminal peptides (N-Trp) show an increase of the static emission intensity as rising the temperature from 10 to about 40 degrees C. the anomaly is typical of the N-Trp terminal peptides since neither tryptophan (Trp) nor glycyl-tryptophan (Gly-Trp) and alanyl-tryptophan (Ala-Trp) show the same trend; a similar behavior is not detected in the C-tryptophan terminals. The other important features are the wavelength and pH dependence of the effect. The anomaly is in fact detected only at neutral pH and for excitation wavelength near the red edge of the UVB absorption band of indole. An interpretation of the anomaly is suggested, though more sophisticated techniques are needed to better focus the problem; the model proposed involves the superimposition of a ground state effect (the temperature-induced equilibrium shift from the zwitterionic to the anionic form of the peptides) and an excited state mechanism. At present no unique interpretation can be provided about the excited state mechanism that favors the anomaly ans some suggestions are discussed.
Brancaleon
L
L
Dipartimento di Fisica, Università di Parma, Viale delle Scienze, 43100 Parma, Ilalia.
Crippa
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PR
Diemmi
D
D
D000595:Amino Acid Sequence; D004151:Dipeptides / Q000737:chemistry; D005453:Fluorescence; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D013696:Temperature; D014364:Tryptophan / Q000737:chemistry*
D004151:Dipeptides; D009842:Oligopeptides; D014364:Tryptophan