Biomolecular Interaction Study of Cyclolinopeptide A with Human Serum Albumin

The kinetics, energetics, and structure of Cyclolinopeptide A binding with Human Serum Albumin were investigated with surface plasmon resonance and circular dichroism. The complex is formed through slow recognition kinetics that is temperature sensitive in the range of 20°C–37°C. The overall reactio...

Descripción completa

Detalles Bibliográficos
Autores principales: Rempel, Ben, Gui, Bo, Maley, Jason, Reaney, Martin, Sammynaiken, Ramaswami
Formato: Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2010
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3062964/
https://www.ncbi.nlm.nih.gov/pubmed/21436992
http://dx.doi.org/10.1155/2010/737289
_version_ 1782200749521895424
author Rempel, Ben
Gui, Bo
Maley, Jason
Reaney, Martin
Sammynaiken, Ramaswami
author_facet Rempel, Ben
Gui, Bo
Maley, Jason
Reaney, Martin
Sammynaiken, Ramaswami
author_sort Rempel, Ben
collection PubMed
description The kinetics, energetics, and structure of Cyclolinopeptide A binding with Human Serum Albumin were investigated with surface plasmon resonance and circular dichroism. The complex is formed through slow recognition kinetics that is temperature sensitive in the range of 20°C–37°C. The overall reaction was observed to be endothermic (ΔH = 204 kJ mol(−1)) and entropy driven (ΔS = 746 J mol(−1)K(−1)) with overall small changes to the tertiary structure.
format Text
id pubmed-3062964
institution National Center for Biotechnology Information
language English
publishDate 2010
publisher Hindawi Publishing Corporation
record_format MEDLINE/PubMed
spelling pubmed-30629642011-03-24 Biomolecular Interaction Study of Cyclolinopeptide A with Human Serum Albumin Rempel, Ben Gui, Bo Maley, Jason Reaney, Martin Sammynaiken, Ramaswami J Biomed Biotechnol Research Article The kinetics, energetics, and structure of Cyclolinopeptide A binding with Human Serum Albumin were investigated with surface plasmon resonance and circular dichroism. The complex is formed through slow recognition kinetics that is temperature sensitive in the range of 20°C–37°C. The overall reaction was observed to be endothermic (ΔH = 204 kJ mol(−1)) and entropy driven (ΔS = 746 J mol(−1)K(−1)) with overall small changes to the tertiary structure. Hindawi Publishing Corporation 2010 2011-03-10 /pmc/articles/PMC3062964/ /pubmed/21436992 http://dx.doi.org/10.1155/2010/737289 Text en Copyright © 2010 Ben Rempel et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Rempel, Ben
Gui, Bo
Maley, Jason
Reaney, Martin
Sammynaiken, Ramaswami
Biomolecular Interaction Study of Cyclolinopeptide A with Human Serum Albumin
title Biomolecular Interaction Study of Cyclolinopeptide A with Human Serum Albumin
title_full Biomolecular Interaction Study of Cyclolinopeptide A with Human Serum Albumin
title_fullStr Biomolecular Interaction Study of Cyclolinopeptide A with Human Serum Albumin
title_full_unstemmed Biomolecular Interaction Study of Cyclolinopeptide A with Human Serum Albumin
title_short Biomolecular Interaction Study of Cyclolinopeptide A with Human Serum Albumin
title_sort biomolecular interaction study of cyclolinopeptide a with human serum albumin
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3062964/
https://www.ncbi.nlm.nih.gov/pubmed/21436992
http://dx.doi.org/10.1155/2010/737289
work_keys_str_mv AT rempelben biomolecularinteractionstudyofcyclolinopeptideawithhumanserumalbumin
AT guibo biomolecularinteractionstudyofcyclolinopeptideawithhumanserumalbumin
AT maleyjason biomolecularinteractionstudyofcyclolinopeptideawithhumanserumalbumin
AT reaneymartin biomolecularinteractionstudyofcyclolinopeptideawithhumanserumalbumin
AT sammynaikenramaswami biomolecularinteractionstudyofcyclolinopeptideawithhumanserumalbumin

Ejemplares similares