English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Entropically driven Polymeric Enzyme Inhibitors by End‐Group directed Conjugation

Hijazi, M., Krumm, C., Cinar, S., Arns, L., Alachraf, M. W., Hiller, W., et al. (2018). Entropically driven Polymeric Enzyme Inhibitors by End‐Group directed Conjugation. Chemistry – A European Journal, 24(18), 4523-4527. doi:10.1002/chem.201800168.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Hijazi, Montasser1, Author
Krumm, Christian1, Author
Cinar, Suelyman2, Author
Arns, Loana2, Author
Alachraf, Mohammed Wasim3, Author           
Hiller, Wolfgang2, Author
Schrader, Wolfgang3, Author           
Winter, Roland2, Author
Tiller, Joerg1, Author
Affiliations:
1Department of Bio- and Chemical Engineering, Technical University of Dortmund, Dortmund, Germany, ou_persistent22              
2Department of Chemistry and Chemical Biology, Physical Chemistry, Technical University of Dortmund, Dortmund, Germany, ou_persistent22              
3Service Department Schrader (MS), Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_1445629              

Content

show
hide
Free keywords: functional polymer end groups; horse radish peroxidase; inhibitors; poly(2-oxazoline)
 Abstract: A new generic concept for polymeric enzyme inhibitors is presented using the example of poly(2‐methyl‐2‐oxazoline) (PMOx) terminated with an iminodiacetate (IDA) function. These polymers are shown to be non‐competitive inhibitors for horseradish peroxidase (HRP). Mechanistic investigations revealed that the polymer is directed to the protein by its end group and collapses at the surface in an entropy‐driven process as shown by isothermal titration calorimetry. The dissociation constant of the complex was determined as the inhibition constant Ki using HRP kinetic activity measurements. Additional experiments suggest that the polymer does not form a diffusion layer around the protein, but might inhibit by inducing minor conformational changes in the protein. This kind of inhibitor offers new avenues towards designing bioactive compounds.

Details

show
hide
Language(s): eng - English
 Dates: 2018-01-122018-01-312018-03-26
 Publication Status: Published online
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/chem.201800168
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Chemistry – A European Journal
  Other : Chem. – Eur. J.
  Other : Chem. Eur. J.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 24 (18) Sequence Number: - Start / End Page: 4523 - 4527 Identifier: ISSN: 0947-6539
CoNE: https://pure.mpg.de/cone/journals/resource/954926979058