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Titration and fluorometric studies of the tyrosine side chain of angiotensin II and related peptides

✍ Scribed by Luiz Juliano; Cecilia Laluce; Maria C. F. Oliveira; Antonio C. M. Paiva

Publisher
Wiley (John Wiley & Sons)
Year
1979
Tongue
English
Weight
750 KB
Volume
18
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

The effect of charged side chains on the ionization and fluorescence of the Tyr^4^ phenolic group in angiotensin (Asp‐Arg‐Val‐Tyr‐Ile‐His‐Pro‐Phe) was investigated. Several synthetic peptides related to angiotensin were titrated spectrophotometrically and quantum yields of tyrosine fluorescence were also determined. The electrostatic interactions were interpreted according to the Kirkwood‐Tanford theory, and the results were related to a recently proposed model [J. L. De Coen and E. Ralston (1977) Biopolymers 16, 1929] for angiotensin conformation in solution. The titration and fluorescence results are in good agreement with the folded conformations of this model, with the exception that the data indicate a weaker interaction between the histidine side chain and the C‐terminal carboxyl groups than that proposed in the model.

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