Contribution of a pyrene fluorescence probe to the aggregation propensity of polypeptides.
[structure: see text] Two synthetic polypeptides, TT1p and TT1b, have been used in comparative aggregation equilibrium studies. The findings reveal that a single alkylpyrene moiety in TT1p contributes about 30% of the polypeptide dimerization energy in aqueous media. This result not only is informative with regard to the aggregation properties of these particular photoactive polypeptides but also provides a quantitative understanding of the limitations on the use of pyrene chromophores as emission probes.
Jones
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Department of Chemistry and Photonics Center, Boston University, Boston, MA 02215, USA. jones@chem.bu.edu
Vullev
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D000465:Algorithms; D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D005456:Fluorescent Dyes / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D010455:Peptides / Q000138:chemical synthesis*; D011721:Pyrenes / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet
D005456:Fluorescent Dyes; D010455:Peptides; D011721:Pyrenes