Time-Resolved Phosphorescence of Tyrosine, Tyrosine Analogs, and Tyrosyl Residues in Oxytocin and Small Peptides View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-11

AUTHORS

K. W. Rousslang, P. J. Reid, D. M. Holloway, D. R. Haynes, J. Dragavon, J. B. A. Ross

ABSTRACT

We present the time-resolved phosphorescence of oxytocin, two oxytocin derivatives, vasopressin and a series of compounds that serve as models for free tyrosine. One of the oxytocin derivatives, desaminodicarbaoxytocin, has the disulfide bridge replaced by an ethylene bridge, and lacks the N-terminus. Similar to the reported fluorescence decays of tyrosine in these peptides, the phosphorescence decays generally are not single exponentials, but can be fit as biexponentials. The decay times for the oxytocin peptides are shorter than for desaminodicarbaoxytocin or the model compounds, and this we attribute to enhanced spin-orbit coupling due to the presence of sulfur. We measured the phosphorescence decay of the model cyclic pentapeptide that contains tyrosine and compared it to that observed for the same cyclic pentapeptide in which tyrosine is replaced by tryptophan. We also report the phosphorescence of 2-tryptophan-oxytocin, and deamino-2-tryptophan-oxytocin in which biexponential phosphorescence decay is also observed. More... »

PAGES

547-555

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1022481706721

DOI

http://dx.doi.org/10.1023/a:1022481706721

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1009269457

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12638657


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