Systematic Measurements of Peptide Adsorption in Hydrophobic Chromatography

2006 ◽  
Vol 51 (1) ◽  
pp. 157-160 ◽  
Author(s):  
Alexander S. Freed ◽  
Kosta Makrodimitris ◽  
John P. O'Connel ◽  
Erik J. Fernandez
Keyword(s):  
Hydrophobic Chromatography ◽  
Peptide Adsorption

scholarly journals Strain-Dependent Adsorption of Pseudomonas aeruginosa-Derived Adhesin-like Peptides at Abiotic Surfaces

Micro ◽  
2021 ◽  
Vol 1 (1) ◽  
pp. 129-139
Author(s):  
Yu Yang ◽  
Sabrina Schwiderek ◽  
Guido Grundmeier ◽  
Adrian Keller
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Molecular Level ◽  
Microbial Colonization ◽  
Peptide Sequence ◽  
Type Iv ◽  
Research Activities ◽  
Abiotic Surfaces ◽  
Peptide Adsorption ◽  
Pilin Protein ◽  
Strain Dependent

Implant-associated infections are an increasingly severe burden on healthcare systems worldwide and many research activities currently focus on inhibiting microbial colonization of biomedically relevant surfaces. To obtain molecular-level understanding of the involved processes and interactions, we investigate the adsorption of synthetic adhesin-like peptide sequences derived from the type IV pili of the Pseudomonas aeruginosa strains PAK and PAO at abiotic model surfaces, i.e., Au, SiO2, and oxidized Ti. These peptides correspond to the sequences of the receptor-binding domain 128–144 of the major pilin protein, which is known to facilitate P. aeruginosa adhesion at biotic and abiotic surfaces. Using quartz crystal microbalance with dissipation monitoring (QCM-D), we find that peptide adsorption is material- as well as strain-dependent. At the Au surface, PAO(128–144) shows drastically stronger adsorption than PAK(128–144), whereas adsorption of both peptides is markedly reduced at the oxide surfaces with less drastic differences between the two sequences. These observations suggest that peptide adsorption is influenced by not only the peptide sequence, but also peptide conformation. Our results furthermore highlight the importance of molecular-level investigations to understand and ultimately control microbial colonization of surfaces.

scholarly journals Hydrophobic chromatography in the resolution of the interconvertible forms of glycogen phosphorylase

FEBS Letters ◽  
1974 ◽  
Vol 40 (1) ◽  
pp. 142-145 ◽  
Author(s):  
Zvi Er-el ◽  
Shmuel Shaltiel
Keyword(s):  
Glycogen Phosphorylase ◽  
Hydrophobic Chromatography

scholarly journals Hydrophobic Chromatography: Use for Purification of Glycogen Synthetase

1973 ◽  
Vol 70 (3) ◽  
pp. 778-781 ◽  
Author(s):  
S. Shaltiel ◽  
Z. Er-El
Keyword(s):  
Hydrophobic Chromatography ◽  
Glycogen Synthetase

Preparation of highly cross-linked raspberry-like nano/microspheres and surface tailoring for controlled immunostimulating peptide adsorption

2016 ◽  
Vol 7 (27) ◽  
pp. 4531-4541 ◽  
Author(s):  
Chunbao Du ◽  
Nan Zhang ◽  
Shichao Ding ◽  
Xumian Gao ◽  
Ping Guan ◽  
...  
Keyword(s):  
Ionic Liquid ◽  
Peptide Adsorption

The surface functionalities of ionic liquid-functionalized nano/microspheres with a highly cross-linked raspberry-like structure could be well controlled by adjusting the functional chains appropriately.

Isolation by hydrophobic chromatography of the chemotactic factor inactivators from human serum

1979 ◽  
Vol 12 (2) ◽  
pp. 162-176 ◽  
Author(s):  
Donald L. Kreutzer ◽  
William D. Claypool ◽  
Michael L. Jones ◽  
Peter A. Ward
Keyword(s):  
Human Serum ◽  
Chemotactic Factor ◽  
Hydrophobic Chromatography

Strategy for Pure Hydrophobic Chromatography

1978 ◽  
pp. 357-362 ◽  
Author(s):  
A. H. Nishikawa
Keyword(s):  
Hydrophobic Chromatography

Separation of soybean lipoxygenase and peroxidase by hydrophobic chromatography

1978 ◽  
Vol 26 (6) ◽  
pp. 1474-1476 ◽  
Author(s):  
William H. Flurkey ◽  
Linda W. Young ◽  
Joseph J. Jen
Keyword(s):  
Soybean Lipoxygenase ◽  
Hydrophobic Chromatography
Sign in / Sign up

Export Citation Format

Share Document