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Comparison of the helix-coil transition of a titrating polypeptide in aqueous solutions and at the air-water interface

Sjögren, Helen LU and Ulvenlund, Stefan LU (2005) In Biophysical Chemistry 116(1). p.11-21
Abstract
The transition from a-helix to random coil of the titrating polyamino acid Co-poly-L-(lysine, phenylalanine), (p-(Lys,Phe)), has been investigated as a function of pH and ionic strength in aqueous solution and at the air water interface by means of circular dichroism (CD) spectroscopy and the Langmuir surface film balance technique. The results strongly suggest that the helix-coil transition for peptides at the air-water interface can be determined by using the two-dimensional Flory exponent, v, to express the pH dependent peptide surface conformation. The helix-coil titration curve of p-(Lys,Phe) shifts approximately 2.5 pH units towards lower pH at the air-water interface, as compared with the bulk solution. This finding is of relevance... (More)
The transition from a-helix to random coil of the titrating polyamino acid Co-poly-L-(lysine, phenylalanine), (p-(Lys,Phe)), has been investigated as a function of pH and ionic strength in aqueous solution and at the air water interface by means of circular dichroism (CD) spectroscopy and the Langmuir surface film balance technique. The results strongly suggest that the helix-coil transition for peptides at the air-water interface can be determined by using the two-dimensional Flory exponent, v, to express the pH dependent peptide surface conformation. The helix-coil titration curve of p-(Lys,Phe) shifts approximately 2.5 pH units towards lower pH at the air-water interface, as compared with the bulk solution. This finding is of relevance for the understanding of conformation and conformational changes of membrane-tran sporting and membrane penetrating peptides as well as for the use of peptides in molecular devices. (c) 2005 Elsevier B.V All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biophysical Chemistry
volume
116
issue
1
pages
11 - 21
publisher
Elsevier
external identifiers
  • wos:000229682500002
  • scopus:19444374318
ISSN
1873-4200
DOI
10.1016/j.bpc.2005.01.007
language
English
LU publication?
yes
id
9af2ef57-e88a-4cd4-88ba-316c030cd486 (old id 157602)
date added to LUP
2007-07-12 11:40:28
date last changed
2017-07-02 04:15:56
@article{9af2ef57-e88a-4cd4-88ba-316c030cd486,
  abstract     = {The transition from a-helix to random coil of the titrating polyamino acid Co-poly-L-(lysine, phenylalanine), (p-(Lys,Phe)), has been investigated as a function of pH and ionic strength in aqueous solution and at the air water interface by means of circular dichroism (CD) spectroscopy and the Langmuir surface film balance technique. The results strongly suggest that the helix-coil transition for peptides at the air-water interface can be determined by using the two-dimensional Flory exponent, v, to express the pH dependent peptide surface conformation. The helix-coil titration curve of p-(Lys,Phe) shifts approximately 2.5 pH units towards lower pH at the air-water interface, as compared with the bulk solution. This finding is of relevance for the understanding of conformation and conformational changes of membrane-tran sporting and membrane penetrating peptides as well as for the use of peptides in molecular devices. (c) 2005 Elsevier B.V All rights reserved.},
  author       = {Sjögren, Helen and Ulvenlund, Stefan},
  issn         = {1873-4200},
  language     = {eng},
  number       = {1},
  pages        = {11--21},
  publisher    = {Elsevier},
  series       = {Biophysical Chemistry},
  title        = {Comparison of the helix-coil transition of a titrating polypeptide in aqueous solutions and at the air-water interface},
  url          = {http://dx.doi.org/10.1016/j.bpc.2005.01.007},
  volume       = {116},
  year         = {2005},
}