NDLI: Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review

Content Provider	Royal Society of Chemistry (RSC)
Author	FitzGerald, Richard J. Nongonierma, Alice B.
Copyright Year	2016
Abstract	The generation of bioactive peptides (BAPs) from dietary proteins has been widely studied. One of the main limitations of a broader application of BAPs in functional foods may arise from their low potency. Therefore, the search for more potent structures is crucial. Quantitative structure–activity relationship (QSAR) has been widely applied in drug discovery and some examples may also be found in the study of BAPs. The aim of this review was to assess the efficiency of QSAR for the discovery of novel and potent BAPs, derived from food protein sources. A wide range of bioactive properties including antioxidant, antimicrobial, angiotensin converting enzyme (ACE), renin and dipeptidyl peptidase IV (DPP-IV) inhibition as well as bitter peptides has been investigated with QSAR. Some studies have identified structural requirements for specific bioactivities, which generally confirmed findings from earlier studies carried out on those BAPs. However, discrepancies are found across analyses, possibly due to the quality of the peptide datasets as well as the descriptors used to build QSAR models. It appears to date that only a limited number of QSAR studies conducted with BAPs have subsequently carried out confirmatory studies and evaluated promising peptide sequences in vivo. This suggests that more research is needed in order to advance knowledge in the area of BAP discovery using QSAR.
Starting Page	75400
Ending Page	75413
Page Count	14
File Format	HTM / HTML PDF
ISSN	20462069
Volume Number	6
Issue Number	79
Journal	RSC Advances
DOI	10.1039/c6ra12738j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Antimicrobial BAP Renin Quantitative structure\u2013activity relationship Drug discovery Angiotensin-converting enzyme Antioxidant Peptide Protein
Content Type	Text
Resource Type	Article
Subject	Chemistry Chemical Engineering

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