Abstract:
: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.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Brancaleon L,Crippa PR,Diemmi Ddoi
10.1002/bip.360360606subject
Has Abstractpub_date
1995-12-01 00:00:00pages
723-33issue
6eissn
0006-3525issn
1097-0282journal_volume
36pub_type
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