English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Devising self-assembled-monolayers for surface-enhanced infrared spectroscopy of pH-driven poly-L-lysine conformational changes

Fallah, M. A., Stanglmair, C., Pacholski, C., & Hauser, K. (2016). Devising self-assembled-monolayers for surface-enhanced infrared spectroscopy of pH-driven poly-L-lysine conformational changes. Langmuir, 32(29), 7356-7364. doi:10.1021/acs.langmuir.6b01742.

Item is

Files

show Files
hide Files
:
langmuir_32_2016_7356.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
langmuir_32_2016_7356.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
Langmuir_32_2016_7356_Suppl.pdf (Supplementary material), 448KB
 
File Permalink:
-
Name:
Langmuir_32_2016_7356_Suppl.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
Description:
-

Creators

show
hide
 Creators:
Fallah, Mohammad A., Author
Stanglmair, Christoph1, Author              
Pacholski, Claudia1, 2, Author              
Hauser, Karin, Author
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              
2Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              

Content

show
hide
Free keywords: Abt. Spatz
 Abstract: Surface-enhanced infrared absorption spectroscopy (SEIRA) is applied to study protein conformational changes. In general, the appropriate functionalization of metal surfaces with biomolecules remains a challenge if the conformation and activity of the biomolecule shall be preserved. Here we present a SEIRA study to monitor pH-induced conformational changes of poly-l-lysine (PLL) covalently bound to a thin gold layer via self-assembled monolayers (SAMs). We demonstrate that the composition of the SAM is crucial. A SAM of 11-mercaptoundecanonic acid (MUA) can link PLL to the gold layer, but pH-driven conformational transitions were hindered compared to poly-l-lysine in solution. To address this problem, we devised a variety of SAMs, i.e., mixed SAMs of MUA with either octanethiol (OT) or 11-mercapto-1-undecanol (MUoL) and furthermore SAMs of MT(PEG)4 and NHS-PEG10k-SH. These mixed SAMs modify the surface properties by changing the polarity and the morphology of the surface present to nearby PLL molecules. Our experiments reveal that mixed SAMs of MUA-MUoL and SAMs of NHS-PEG10k-SH-MT(PEG)4 are suitable to monitor pH-driven conformational changes of immobilized PLL. These SAMs might be applicable for chemoselective protein immobilization in general.

Details

show
hide
Language(s): eng - English
 Dates: 2016-06-182016-05-072016-07-072016-07-07
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1021/acs.langmuir.6b01742
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Langmuir
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Columbus, OH : American Chemical Society
Pages: - Volume / Issue: 32 (29) Sequence Number: - Start / End Page: 7356 - 7364 Identifier: ISSN: 0743-7463
CoNE: https://pure.mpg.de/cone/journals/resource/954925541194