Publication detail

The effect of hyaluronan on the aggregation of hydrophobized amino acids - a fluorescence study

HALASOVÁ, T. MRAVEC, F. PEKAŘ, M.

Original Title

The effect of hyaluronan on the aggregation of hydrophobized amino acids - a fluorescence study

English Title

The effect of hyaluronan on the aggregation of hydrophobized amino acids - a fluorescence study

Type

journal article - other

Language

en

Original Abstract

The influence of the addition of native hyaluronan of different molecular weights (1.36 MDa and 106 kDa) on the aggregation behavior of hydrophobically modified amino acids in aqueous solution and in 0.15 M NaCl was investigated using pyrene as a solubilization probe. Hyaluronan decreased the critical aggregation concentration in aqueous solution in the case of amino acids modified by a single alkyl chain whereas no change was observed in physiological solution. The aggregation of amino acids modified by two alkyl chains was insensitive to the presence of hyaluronan.

English abstract

The influence of the addition of native hyaluronan of different molecular weights (1.36 MDa and 106 kDa) on the aggregation behavior of hydrophobically modified amino acids in aqueous solution and in 0.15 M NaCl was investigated using pyrene as a solubilization probe. Hyaluronan decreased the critical aggregation concentration in aqueous solution in the case of amino acids modified by a single alkyl chain whereas no change was observed in physiological solution. The aggregation of amino acids modified by two alkyl chains was insensitive to the presence of hyaluronan.

Keywords

hydrophobically modified amino acids, hyaluronan, aggregation, interactions

RIV year

2013

Released

20.05.2013

Pages from

34

Pages to

37

Pages count

4

BibTex


@article{BUT100014,
  author="Tereza {Venerová} and Filip {Mravec} and Miloslav {Pekař}",
  title="The effect of hyaluronan on the aggregation of hydrophobized amino acids - a fluorescence study",
  annote="The influence of the addition of native hyaluronan of different molecular weights (1.36 MDa and 106 kDa) on the aggregation behavior of hydrophobically modified amino acids in aqueous solution and in 0.15 M NaCl was investigated using pyrene as a solubilization probe. Hyaluronan decreased the critical aggregation concentration in aqueous solution in the case of amino acids modified by a single alkyl chain whereas no change was observed in physiological solution. The aggregation of amino acids modified by two alkyl chains was insensitive to the presence of hyaluronan.",
  chapter="100014",
  number="1",
  volume="97",
  year="2013",
  month="may",
  pages="34--37",
  type="journal article - other"
}