Document Detail


Protein stabilization with a dipeptide-mimic triazine-scaffolded synthetic affinity ligand.
MedLine Citation:
PMID:  23334918     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Protein stabilization was achieved by a novel approach based on the adsorption and establishment of affinity-like interactions with a biomimetic triazine-scaffolded ligand. A synthetic lead compound (ligand 3'/11, K(a)  ≈ 10(4)  M(-1) ) was selected from a previously screened solid-phase library of affinity ligands for studies of adsorption and stabilization of cutinase from Fusarium solani pisi used as a model system. This ligand, directly synthesized in agarose by a well-established solid-phase synthesis method, was able to strongly bind cutinase and led to impressive half-lives of more than 8 h at 70 °C, and of approximately 34 h at 60 °C for bound protein (a 25- and 57-fold increase as compared with the free enzyme, respectively). The ligand density in the solid matrix was found to be a determinant parameter for cutinase stabilization. It is conceivable that the highly stabilizing effect observed results from the binding of more than one ligand residue to the enzyme, creating specific macromolecular configurations that lock structural mobility thus improving molecular stability. Copyright © 2013 John Wiley & Sons, Ltd.
Authors:
I T Sousa; N M T Lourenço; C A M Afonso; M A Taipa
Related Documents :
21874338 - A secure lightweight rfid binding proof protocol for medication errors and patient safety.
15006678 - A database of [(18)f]-altanserin binding to 5-ht(2a) receptors in normal volunteers: no...
2996538 - Muramyl peptides and serotonin interact at specific binding sites on macrophages and en...
9699688 - In vivo association between alcohol intoxication, aggression, and serotonin transporter...
16751338 - G-protein-coupled receptor microarrays for multiplexed compound screening.
11700038 - Use of surface plasmon resonance for real-time analysis of the interaction of zo-1 and ...
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of molecular recognition : JMR     Volume:  26     ISSN:  1099-1352     ISO Abbreviation:  J. Mol. Recognit.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9004580     Medline TA:  J Mol Recognit     Country:  England    
Other Details:
Languages:  eng     Pagination:  104-12     Citation Subset:  IM    
Copyright Information:
Copyright © 2013 John Wiley & Sons, Ltd.
Affiliation:
Institute for Biotechnology and Bioengineering, Centro de Engenharia Biológica e Química, Instituto Superior Técnico, Av. Rovisco Pais, 1049-001, Lisboa, Portugal.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Allostery mediates ligand binding to Grb2 adaptor in a mutually exclusive manner.
Next Document:  Asymmetric structure and domain binding interfaces of human tyrosyl-tRNA synthetase studied by molec...