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Combinatorial Methodology. Screening for affinity specific ligands to biological and artificial receptors.

Krook, Margareta LU (1998)
Abstract
Combinatorial screening methodology has been employed to select new affinity specific ligands to bilogical and artificial receptors. The screening methodology, in particular screening of combinatorial phage display peptide libraries against target molecules differing in function and shape, is focused upon.



A linear combinatorial phage display hexapeptide library has been used to select novel peptides interacting with single stranded DNA, an oligonucleotide consisting of seven cytosines. The ability of a small peptide to act as specific recognition element to single stranded DNA is discussed.



Linear hexapeptides interacting with surface structures not involved in the biologically active site on... (More)
Combinatorial screening methodology has been employed to select new affinity specific ligands to bilogical and artificial receptors. The screening methodology, in particular screening of combinatorial phage display peptide libraries against target molecules differing in function and shape, is focused upon.



A linear combinatorial phage display hexapeptide library has been used to select novel peptides interacting with single stranded DNA, an oligonucleotide consisting of seven cytosines. The ability of a small peptide to act as specific recognition element to single stranded DNA is discussed.



Linear hexapeptides interacting with surface structures not involved in the biologically active site on alpha-chymotrypsin were selected using phage display technology. The use of such peptides in analysis and separation applications is discussed.



A novel cyclic peptide functioning as a specific inhibitor to the enzyme alpha-chymotrypsin has been selected from a random phage display nonapeptide library and characterized. The importance of conformation of the peptide on the inhibiting capacity is demonstrated.



Peptides interacting with the invariable regions (Fc) of immunoglobulins have been selected from a phage display decapeptide library. The peptids have been shown to exhibit varying specificities to immunoglobulins from different subclasses and immunoglobulins originating from different species. The use of such peptides i analysis and separation applications is discussed.



In addition, via the conceptof Molecular Imprinting Technology, a method which involves casting a polymeric network around a template molecule leaving a cavity or imprint when removed, the production of new polymeric artificial target molecules to be used in screening applications is demonstrated. Molecular imprinting technology has been used to prepare artificial polymeric steroid receptors for screening a combinatorial steroid library. (Less)
Please use this url to cite or link to this publication:
author
opponent
  • Ruoslahti, Erkki, M.D., President and CEO, The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, California 92037, USA
organization
publishing date
type
Thesis
publication status
published
subject
keywords
peptide library, combinatorial, screening, phage display, affinity, DNA-interaction, chymotrypsin, peptide inhibitor, antibody, IgG, Fc, molecular imprinting, steroid, receptor, Biochemistry, Metabolism, Biokemi, Biotechnology, Bioteknik
pages
150 pages
publisher
Pure and Applied Biochemistry, Lund University
defense location
room C at the Center for Chemistry and Chemical Engineering, Sölvegatan 39, Lund
defense date
1998-04-17 10:15
external identifiers
  • Other:LUTKDH/TKBK-1043/1-150/1998
ISBN
91-628-2946-7
language
English
LU publication?
yes
id
50f10f2d-5b76-417b-9e9d-2f1a09277daf (old id 38510)
date added to LUP
2007-08-01 11:43:45
date last changed
2016-09-19 08:45:06
@phdthesis{50f10f2d-5b76-417b-9e9d-2f1a09277daf,
  abstract     = {Combinatorial screening methodology has been employed to select new affinity specific ligands to bilogical and artificial receptors. The screening methodology, in particular screening of combinatorial phage display peptide libraries against target molecules differing in function and shape, is focused upon.<br/><br>
<br/><br>
A linear combinatorial phage display hexapeptide library has been used to select novel peptides interacting with single stranded DNA, an oligonucleotide consisting of seven cytosines. The ability of a small peptide to act as specific recognition element to single stranded DNA is discussed.<br/><br>
<br/><br>
Linear hexapeptides interacting with surface structures not involved in the biologically active site on alpha-chymotrypsin were selected using phage display technology. The use of such peptides in analysis and separation applications is discussed.<br/><br>
<br/><br>
A novel cyclic peptide functioning as a specific inhibitor to the enzyme alpha-chymotrypsin has been selected from a random phage display nonapeptide library and characterized. The importance of conformation of the peptide on the inhibiting capacity is demonstrated.<br/><br>
<br/><br>
Peptides interacting with the invariable regions (Fc) of immunoglobulins have been selected from a phage display decapeptide library. The peptids have been shown to exhibit varying specificities to immunoglobulins from different subclasses and immunoglobulins originating from different species. The use of such peptides i analysis and separation applications is discussed.<br/><br>
<br/><br>
In addition, via the conceptof Molecular Imprinting Technology, a method which involves casting a polymeric network around a template molecule leaving a cavity or imprint when removed, the production of new polymeric artificial target molecules to be used in screening applications is demonstrated. Molecular imprinting technology has been used to prepare artificial polymeric steroid receptors for screening a combinatorial steroid library.},
  author       = {Krook, Margareta},
  isbn         = {91-628-2946-7},
  keyword      = {peptide library,combinatorial,screening,phage display,affinity,DNA-interaction,chymotrypsin,peptide inhibitor,antibody,IgG,Fc,molecular imprinting,steroid,receptor,Biochemistry,Metabolism,Biokemi,Biotechnology,Bioteknik},
  language     = {eng},
  pages        = {150},
  publisher    = {Pure and Applied Biochemistry, Lund University},
  school       = {Lund University},
  title        = {Combinatorial Methodology. Screening for affinity specific ligands to biological and artificial receptors.},
  year         = {1998},
}