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Therefore, diet designs for chronic disease management will have to consider thermal processing-linked modification of bioactive ingredient profiles.
Here, the silane coupling agent KH560 [γ- 2,3-epoxypropoxy propyltrimethoxysilane] is used for graft modification of bioactive HA (hydroxyapatite) particles and for preparing HA/PEEK composites via a hot-press molding method.
Three main coupling strategies for linking IONPs with active agents are presented: (i) chemical modification of amine groups on the surface of IONPs, (ii) chemical modification of bioactive substances (e.g. with fluorescent dyes), and (iii) the activation of carboxyl groups mainly for enzyme immobilization.
Structural modification of bioactive natural products according to combination principle was an important approach in search for new lead compounds [7 9].
Not only cross-reactivity but also differences in subcellular localization of DPPIV (i.e. secretory endosomes or plasma membrane) may have important consequences for T cell reactivity and pre-secretion modification of bioactive peptides.
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Peptidomimetic structures represent a useful tool in drug discovery, as modifications of bioactive peptides can result in better pharmacological properties, such as higher metabolic stability, increased bioavailability, and higher receptor affinity or selectivity.
The enzymatic transglycosylation by dextransucrase from Leuconostoc mesenteroides has been previously used for the modification of various bioactive compounds to improve their function or physical stability (Moon et al. 2007a; Seo et al. 2009).
Nevertheless, resistant mutant selection of MDR-sup S. pombe provides the means for developing mode of action hypotheses that do not require any chemical modification of the bioactive compound, preliminary prediction of the target, or construction of a custom-made genetic library, thereby serving as a convenient alternative approach for target identification studies of cytotoxic natural products.
It has been hypothesised that this generic action is due to the modification allowing release of bioactive fragment(s) which are claimed to bind specifically to and inhibit the action of the mammalian lectin galectin 3 (Gal3).
J. L. West, "Modification of Materials With Bioactive Peptides", in Biopolymer Methods in Tissue Engineering, vol. 238, A. P. Hollander and Hatton, P. V. New Jersey: Humana Press, 2003, pp. 113 - 122.
In the light of our ongoing study, the modification of biomaterials with bioactive molecules [ 27, 28], such as a native long chain proteins or short peptide sequences derived from intact ECM proteins, that can incur specific interactions with cell receptors should benefit from the description of biological characteristics of cells in the presence of naturally derived cardiac ECM.
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